FTIR analysis of natural and synthetic collagen
Abstract
Collagen is the most abundant protein in humans and animals, comprising of one third of the total proteins that accounts for three quarters of the dry weight skin in humans. Collagen containing a range of proteins has been reported for tissue engineering applications, but, only a small number of studies related to chemical structure evaluation of collagen are found in the literature. Collagen can be obtained from both the natural and synthetic sources and offers a wide range of biomedical applications due to its excellent biocompatibility and low immunogenicity. Hence, it is important to identify chemical structural properties of collagen and Fourier transform infrared (FTIR) appears to be a technique of choice to study their chemical structure. This review aims to highlight the use of FTIR to study collagen-based biomaterials, using it for characterization of collagen extracted from various sources. Characterization of collagen-based materials used in wound healing, skin substitutes, derma fillers, and aging of skin, collagen containing drug delivery agents, collagen-based materials used in tissue engineering, bone regeneration, and osteogenic differentiation is discussed in detail. FTIR analysis of collagen-containing materials used for dental applications, cleft-palate, and in alveolar-ridge preservation has also been highlighted.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The FTIR spectrum of pure type I collagen exhibits characteristic absorption bands: amide I at approximately 1642 cm−1, amide II at 1537 cm−1, and amide III at 1236 cm−1.
“The strong band centered at approximately 1642 cm⁻¹ is assigned to the amide I vibration, predominantly arising from C=O stretching of the peptide backbone and highly sensitive to collagen secondary structure.”
Cites
Infrared spectroscopy of proteins
Barth, A. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.06.004 · Cited by 5,129 · cited 1× · see citing works
“1253 cm¡1, His’ v(CN) and d(CH) at 1104, 1090, 1106, and 1094 cm¡1, Thr’s n(CO) at 1075–1150 cm¡1 (NC) at 1092 cm¡1, Ser’s v(CO) or v(CC) at 983 cm¡1, v(NC), d(CH), and v(CC) at 1064 cm¡1, gt CH2 at 1063–1295 cm¡1, v(CC) and d (CH) at 1012–1016 cm¡1 (157).”
Alberts, B., Johnson, A. D., Lewis, J. H., RAFF, M. C., Roberts, K. J., & Walter, P. (2007) · W.W. Norton eBooks · doi:10.1201/9780203833445 · Cited by 4,591 · see citing works
Fourier Transform Infrared Spectroscopic Analysis of Protein Secondary Structures
Kong, J., & Yu, S. (2007) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2007.00320.x · Cited by 3,544 · see citing works
Perfusion-decellularized matrix: using nature's platform to engineer a bioartificial heart
Ott, H. C., Matthiesen, T. S., Goh, S.-K., Black, L. D., Kren, S. M., Netoff, T. I., & Taylor, D. A. (2008) · Nature Medicine · doi:10.1038/nm1684 · Cited by 2,650 · see citing works
Interactions between Alginate and Chitosan Biopolymers Characterized Using FTIR and XPS
Lawrie, G. A., Keen, I., Drew, B., Chandler-Temple, A. F., Rintoul, L., Fredericks, P. M., & Grøndahl, L. (2007) · Biomacromolecules · doi:10.1021/bm070014y · Cited by 1,427 · see citing works
UV-light-induced signal cascades and skin aging
Rittié, L. (2002) · Ageing Research Reviews · doi:10.1016/s1568-1637(02)00024-7 · Cited by 987 · see citing works
Muyonga, J. H., Cole, C., & Duodu, K. G. (2004) · Food Chemistry · doi:10.1016/j.foodchem.2003.09.038 · Cited by 905 · see citing works
Characterisation of acid soluble collagen from skins of young and adult Nile perch (Lates niloticus)
Muyonga, J. H., Cole, C., & Duodu, K. G. (2003) · Food Chemistry · doi:10.1016/j.foodchem.2003.06.006 · Cited by 624 · see citing works
Periodate Oxidation of Crystalline Cellulose
Kim, U., Kuga, S., Wada, M., Okano, T., & Kondo, T. (2000) · Biomacromolecules · doi:10.1021/bm0000337 · Cited by 624 · see citing works
Collagen types analysis and differentiation by FTIR spectroscopy
Belbachir, K., Noreen, R., Gouspillou, G., & Petibois, C. (2009) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-009-3019-y · Cited by 564 · see citing works
FT-IR study for hydroxyapatite/collagen nanocomposite cross-linked by glutaraldehyde
Chang, M. C., & Tanaka, J. (2002) · Biomaterials · doi:10.1016/s0142-9612(02)00232-6 · Cited by 560 · see citing works
Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus)
Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., Nagai, T., & Tanaka, M. (2004) · Food Chemistry · doi:10.1016/j.foodchem.2004.02.042 · Cited by 534 · see citing works
FT-IR imaging of native and tissue-engineered bone and cartilage
Boskey, A. L., & Pleshko, N. L. (2006) · Biomaterials · doi:10.1016/j.biomaterials.2006.11.043 · Cited by 533 · see citing works
Spectroscopic Characterization of Collagen Cross-Links in Bone
Paschalis, E. P., Verdelis, K., Doty, S. B., Boskey, A. L., Mendelsohn, R., & Yamauchi, M. (2001) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.2001.16.10.1821 · Cited by 518 · see citing works
Molecular interactions in collagen and chitosan blends
Sionkowska, A., Wisniewski, M., Skopińska-Wiśniewska, J., et al. (2003) · Biomaterials · doi:10.1016/s0142-9612(03)00595-7 · Cited by 514 · see citing works
Collagen type I amide I band infrared spectroscopy
Vidal, B. D. C., & Mello, M. L. S. (2010) · Micron · doi:10.1016/j.micron.2010.09.010 · Cited by 447 · see citing works
Collagen scaffolds derived from a marine source and their biocompatibility
Song, E. J., Kim, S. Y., Chun, T., Byun, H.-J., & Lee, Y. M. (2006) · Biomaterials · doi:10.1016/j.biomaterials.2006.01.015 · Cited by 409 · see citing works
Liu, L., Li, C., Bao, C., Jia, Q., Xiao, P., Liu, X., & Zhang, Q. (2012) · Talanta · doi:10.1016/j.talanta.2012.02.051 · Cited by 408 · see citing works
The application of recombinant human collagen in tissue engineering
Yang, C., Hillas, P. J., B??ez, J. A., Nokelainen, M., Balan, J., Tang, J., Spiro, R., & Polarek, J. W. (2004) · BioDrugs · doi:10.2165/00063030-200418020-00004 · Cited by 385 · see citing works
Chen, Z. G., Wang, P. W., Wei, B., Mo, X. M., & Cui, F. (2009) · Acta Biomaterialia · doi:10.1016/j.actbio.2009.07.024 · Cited by 380 · see citing works
Archibald, S. J., Krarup, C., Shefner, J. M., Li, S., & Madison, R. D. (1991) · The Journal of Comparative Neurology · doi:10.1002/cne.903060410 · Cited by 375 · see citing works
Arkhipkin, A. I., Rodhouse, P. G., Pierce, G. J., Sauer, W., Sakai, M., Allcock, A. L., Argüelles, J., BOWER, J. R. F., Castillo, G., Ceriola, L., et al. (2015) · Reviews in Fisheries Science & Aquaculture · doi:10.1080/23308249.2015.1026226 · Cited by 352 · see citing works
Collagen–chitosan polymeric scaffolds for the in vitro culture of human epidermoid carcinoma cells
Natesan, S., Ravichandran, P. K., Reddy, P. N., et al. (2001) · Biomaterials · doi:10.1016/s0142-9612(00)00220-9 · Cited by 341 · see citing works
Crosslinked collagen/chitosan matrix for artificial livers
Wang, X. H., Li, D. P., Wang, W. J., Feng, Q., Cui, F. Z., Xu, Y., Xu, S., & van der Werf, M. (2003) · Biomaterials · doi:10.1016/s0142-9612(03)00170-4 · Cited by 321 · see citing works
Li, Z., Wang, B., Chi, C., Zhang, Q., Gong, Y., Tang, J., Luo, H., & Ding, G. (2012) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2012.10.001 · Cited by 315 · see citing works
FTIR characterization of protein–polysaccharide interactions in extruded blends
Guerrero, P., Kerry, J. P., & de la Caba, K. (2014) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2014.05.005 · Cited by 301 · see citing works
Intermolecular interactions in electrospun collagen–chitosan complex nanofibers
Chen, Z., Mo, X., He, C., et al. (2007) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2007.09.018 · Cited by 285 · see citing works
Matmaroh, K., Benjakul, S., Prodpran, T., Encarnacion, A. B., & Kishimura, H. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2011.05.099 · Cited by 280 · see citing works
Huang, C.-Y., Kuo, J., Wu, S.-J., & Tsai, H.-T. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.06.066 · Cited by 264 · see citing works
Collagen-based wound dressing: Effects of hyaluronic acid and firponectin on wound healing
Doillon, C. J., & Silver, F. H. (1986) · Biomaterials · doi:10.1016/0142-9612(86)90080-3 · Cited by 247 · see citing works
Therapeutic potential of RNA interference against cancer
Takeshita, F., & Ochiya, T. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00234.x · Cited by 239 · see citing works
Wang, L., An, X., Yang, F., Xin, Z., Zhao, L., & Hu, Q. (2007) · Food Chemistry · doi:10.1016/j.foodchem.2007.11.017 · Cited by 233 · see citing works
Collagen structural hierarchy and susceptibility to degradation by ultraviolet radiation
Rabotyagova, O. S., Cebe, P., & Kaplan, D. L. (2008) · Materials Science and Engineering C · doi:10.1016/j.msec.2008.03.012 · Cited by 232 · see citing works
Electrospinning of collagen–chitosan complex
Chen, Z., Mo, X., & Qing, F. (2006) · Materials Letters · doi:10.1016/j.matlet.2006.11.104 · Cited by 231 · see citing works
Chen, J., Li, L., Yi, R., et al. (2015) · LWT · doi:10.1016/j.lwt.2015.10.070 · Cited by 228 · see citing works
Electrospinning of Collagen Nanofiber Scaffolds from Benign Solvents
Dong, B., Arnoult, O., Smith, M., & Wnek, G. E. (2009) · Macromolecular Rapid Communications · doi:10.1002/marc.200800634 · Cited by 228 · see citing works
Chamberlain, L. J., Yannas, I. V., Hsu, H.-P., et al. (1998) · Experimental Neurology · doi:10.1006/exnr.1998.6955 · Cited by 221 · see citing works
Hyaluronic Acid Fillers: A Comprehensive Review
Beasley, K. L., Weiss, M. A., & Weiss, R. A. (2009) · Facial Plastic Surgery · doi:10.1055/s-0029-1220647 · Cited by 221 · see citing works
Exposito, J., Cluzel, C., Garrone, R., & Lethias, C. (2002) · The Anatomical Record · doi:10.1002/ar.10162 · Cited by 206 · see citing works
Veeruraj, A., Arumugam, M., & Balasubramanian, T. (2013) · Process Biochemistry · doi:10.1016/j.procbio.2013.07.011 · Cited by 205 · see citing works
Cunniffe, G. M., Dickson, G. R., Partap, S., Stanton, K. T., & O’Brien, F. J. (2010) · Journal of Materials Science: Materials in Medicine · doi:10.1007/s10856-009-3964-1 · Cited by 199 · see citing works
Cheng, X., Shao, Z., Li, C., Yu, L., Raja, M. A., & Liu, C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169731 · Cited by 199 · see citing works
Structure Determination of Organic Compounds
Pretsch, E., Bühlmann, P., & Badertscher, M. (2020) · Springer eBooks · doi:10.1007/978-3-662-62439-5 · Cited by 195 · see citing works
Morishita, M., Goto, T., Nakamura, K., Lowman, A. M., Takayama, K., & Peppas, N. A. (2005) · Journal of Controlled Release · doi:10.1016/j.jconrel.2005.10.029 · Cited by 191 · see citing works
Atelocollagen for protein and gene delivery
Sano, A. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2003.08.005 · Cited by 188 · see citing works
Modification of collagen with a natural derived cross-linker, alginate dialdehyde
Hu, Y., Liu, L., Gu, Z., Dan, W., Dan, N., & Yu, X. (2013) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2013.11.050 · Cited by 181 · see citing works
Grdadolnik, J., & Mar�chal, Y. (2000) · Biopolymers · doi:10.1002/1097-0282(2001)62:1 · Cited by 172 · see citing works
Cytocompatibility of chitosan and collagen-chitosan scaffolds for tissue engineering
Fernandes, L. L., Resende, C. X., Tavares, D. D. S., et al. (2011) · Polímeros · doi:10.1590/s0104-14282011005000008 · Cited by 171 · see citing works
Liu, D., Wei, G., Li, T., Hu, J., Lu, N., Regenstein, J. M., & Zhou, P. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.09.147 · Cited by 170 · see citing works
Characteristics of collagens from the swim bladders of yellowfin tuna (Thunnus albacares)
Kaewdang, O., Benjakul, S., Kaewmanee, T., & Kishimura, H. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.01.076 · Cited by 169 · see citing works
Bacterial Cellulose/Collagen Hydrogel for Wound Healing
Moraes, P. R. F. D. S., Saska, S., Barud, H. D. S., Lima, L. R., Martins, V. D. C. A., Plepis, A. M. D. G., Ribeiro, S. J. L., & Gaspar, A. M. M. (2016) · Materials Research · doi:10.1590/1980-5373-mr-2015-0249 · Cited by 167 · see citing works
Layered chitosan-collagen hydrogel/aligned PLLA nanofiber construct for flexor tendon regeneration
Deepthi, S., Sundaram, M. N., Kadavan, J. D., et al. (2016) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2016.07.124 · Cited by 166 · see citing works
Kansiz, M., Billman‐Jacobe, H., & McNaughton, D. (2000) · Applied and Environmental Microbiology · doi:10.1128/aem.66.8.3415-3420.2000 · Cited by 160 · see citing works
Taravel, M. N., & Domard, A. (1993) · Biomaterials · doi:10.1016/0142-9612(93)90135-o · Cited by 157 · see citing works
Sundaramurthy, A., Krishnamoorthy, G., Ramkumar, K. M., et al. (2016) · Materials Science and Engineering C · doi:10.1016/j.msec.2016.09.003 · Cited by 153 · see citing works
Isolation and characterization of collagen from the outer skin of squid (Doryteuthis singhalensis)
Veeruraj, A., Arumugam, M., Ajithkumar, T., & Balasubramanian, T. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.07.025 · Cited by 152 · see citing works
Harley, B. A. C., Lynn, A. K., Wissner-Gross, Z. D., Bonfield, W., Yannas, I. V., & Gibson, L. J. (2009) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.32361 · Cited by 152 · see citing works
Three-Dimensional Mineralization of Dense Nanofibrillar Collagen−Bioglass Hybrid Scaffolds
Marelli, B., Ghezzi, C. E., Barralet, J. E., Boccaccini, A. R., & Nazhat, S. N. (2010) · Biomacromolecules · doi:10.1021/bm1001087 · Cited by 152 · see citing works
Chandika, P., Ko, S., Oh, G., Heo, S., Nguyen, V.-T., Jeon, Y., Lee, B., Jang, C. H., Kim, G., Park, W. S., et al. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.08.038 · Cited by 149 · see citing works
Nucleation Sites of Calcium Phosphate Crystals during Collagen Mineralization
Zhang, W., Huang, Z., Liao, S., et al. (2003) · Journal of the American Ceramic Society · doi:10.1111/j.1151-2916.2003.tb03422.x · Cited by 145 · see citing works
The Pursuit of a Scalable Nanofabrication Platform for Use in Material and Life Science Applications
Gratton, S. E. A., Williams, S., Napier, M. E., Pohlhaus, P. D., Zhou, Z., Wiles, K. B., Maynor, B. W., Shen, C. K.-F., Olafsen, T., Samulski, E. T., et al. (2008) · Accounts of Chemical Research · doi:10.1021/ar8000348 · Cited by 142 · see citing works
Solar ultraviolet radiation as a trigger of cell signal transduction
Heck, D. E., Gerecke, D. R., Vetrano, A. M., & Laskin, J. D. (2003) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2003.09.028 · Cited by 141 · see citing works
Characterization of collagen from the skin of Amur sturgeon (Acipenser schrenckii)
Wang, L., Liang, Q., Chen, T., Wang, Z., Xu, J., & Ma, H. (2013) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2013.12.002 · Cited by 141 · see citing works
Tangsadthakun, C., Kanokpanont, S., Sanchavanakit, N., et al. (2006) · Journal of Biomaterials Science Polymer Edition · doi:10.1163/156856207779116694 · Cited by 141 · see citing works
Effect of UV radiation on the infrared spectra of collagen
KAMINSKA, A., & Sionkowska, A. (1996) · Polymer Degradation and Stability · doi:10.1016/0141-3910(95)00159-x · Cited by 139 · see citing works
Chen, J., & Chang, Y.-S. (2011) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2011.03.038 · Cited by 138 · see citing works
Rusa, C. C., & Tonelli, A. E. (2000) · Macromolecules · doi:10.1021/ma000746h · Cited by 136 · see citing works
Zhang, Q., Wang, Q., Lv, S., Lu, J., Jiang, S., Regenstein, J. M., & Lin, L. (2015) · Food Bioscience · doi:10.1016/j.fbio.2015.12.005 · Cited by 132 · see citing works
Characteristics of acid- and pepsin-soluble collagens from scale of seabass (Lates calcarifer)
Chuaychan, S., Benjakul, S., & Kishimura, H. (2015) · LWT · doi:10.1016/j.lwt.2015.03.002 · Cited by 129 · see citing works
Collagen/silk fibroin composite scaffold incorporated with PLGA microsphere for cartilage repair
Wang, J., Qiu, Y., Cheng, N., Tao, X., Zhang, Z., Sun, X., & Zhang, Q. (2016) · Materials Science and Engineering C · doi:10.1016/j.msec.2015.12.097 · Cited by 128 · see citing works
Effect of fish collagen modification on its thermal and rheological properties
Safandowska, M., & Pietrucha, K. (2012) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2012.10.026 · Cited by 123 · see citing works
Chen, S., Chen, H., Xie, Q., Hong, B., Chen, J., Hua, F., Bai, K., He, J., Yi, R., & Wu, H. (2015) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2015.07.027 · Cited by 122 · see citing works
Liang, Q., Wang, L., Sun, W., et al. (2013) · Process Biochemistry · doi:10.1016/j.procbio.2013.12.003 · Cited by 118 · see citing works
Tamilmozhi, S., Veeruraj, A., & Arumugam, M. (2013) · Food Research International · doi:10.1016/j.foodres.2013.10.002 · Cited by 114 · see citing works
Fauzi, M. B., Lokanathan, Y., Aminuddin, B. S., Ruszymah, B. H. I., & Chowdhury, S. R. (2016) · Materials Science and Engineering C · doi:10.1016/j.msec.2016.05.109 · Cited by 114 · see citing works
Northern pike ( Esox lucius ) collagen: Extraction, characterization and potential application
Kozłowska, J., Sionkowska, A., Skopińska-Wiśniewska, J., et al. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.08.002 · Cited by 113 · see citing works
The in vivo bone formation by mesenchymal stem cells in zein scaffolds
Tu, J., Wang, H., Li, H., et al. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2009.04.054 · Cited by 112 · see citing works
Surface modification of electrospun PLGA scaffold with collagen for bioengineered skin substitutes
Sadeghi, A. R., Nokhasteh, S., Molavi, A. M., Khorsand-Ghayeni, M., Naderi‐Meshkin, H., & Mahdizadeh, A. (2016) · Materials Science and Engineering C · doi:10.1016/j.msec.2016.04.073 · Cited by 108 · see citing works
Structural and dynamic properties of water around acetylcholinesterase
Henchman, R. H., & McCammon, J. A. (2002) · Protein Science · doi:10.1110/ps.0214002 · Cited by 107 · see citing works
Zhang, J., Duan, R., Huang, L., et al. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.10.116 · Cited by 102 · see citing works
Isolation and characterisation of collagen from the ribbon jellyfish ( C hrysaora sp.)
Barzideh, Z., Latiff, A. A., Gan, C., Benjakul, S., & Karim, A. A. (2013) · International Journal of Food Science & Technology · doi:10.1111/ijfs.12464 · Cited by 101 · see citing works
Jana, P., Mitra, T., Selvaraj, T. K. R., et al. (2016) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2016.07.053 · Cited by 98 · see citing works
Murali, R., Thanikaivelan, P., & Kalirajan, C. (2014) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2014.08.045 · Cited by 97 · see citing works
A novel composite of collagen-hydroxyapatite/kappa-carrageenan
Feng, W., Feng, S., Tang, K., He, X., Jing, A., & Liang, G. (2016) · Journal of Alloys and Compounds · doi:10.1016/j.jallcom.2016.09.234 · Cited by 94 · see citing works
Mulder, G., Tallis, A. J., Marshall, V. T., Mozingo, D. W., Phillips, L., Pierce, G. F., Chandler, L. A., & Sosnowski, B. K. (2009) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2009.00541.x · Cited by 91 · see citing works
Mitra, T., Jana, P., Raja, S. T. K., Gnanamani, A., & Kundu, P. P. (2015) · RSC Advances · doi:10.1039/c5ra15726a · Cited by 90 · see citing works
Characterization and tissue incorporation of cross-linked human acellular dermal matrix
Lee, J. H., Kim, H. G., & Lee, W. J. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2014.12.004 · Cited by 89 · see citing works
Collagen-based new bioartificial polymeric materials
Giusti, P., Lazzeri, L., Petris, S. D., et al. (1994) · Biomaterials · doi:10.1016/0142-9612(94)90274-7 · Cited by 89 · see citing works
Raman spectroscopic study of glutaraldehyde-stabilized collagen and pericardium tissue
Jastrzebska, M. M., Wrzalik, R., Kocot, A., et al. (2003) · Journal of Biomaterials Science Polymer Edition · doi:10.1163/156856203321142605 · Cited by 87 · see citing works
Short chain collagens in sponges are encoded by a family of closely related genes.
Exposito, J., Guellec, D. L., Lu, Q., & Garrone, R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54725-6 · Cited by 86 · see citing works
Ramasamy, P., & Shanmugam, A. (2014) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2014.11.034 · Cited by 86 · see citing works
Santos, M. H., Menezes‐Silva, R., Dumont, V. C., Neves, J. S., Mansur, H. S., & Heneine, L. G. D. (2012) · Materials Science and Engineering C · doi:10.1016/j.msec.2012.11.003 · Cited by 83 · see citing works
Zhong, M., Chen, T., Hu, C., et al. (2015) · Journal of Food Science · doi:10.1111/1750-3841.12826 · Cited by 82 · see citing works
Characterisation of acid-soluble collagen from skin of silver carp (Hypophthalmichthys molitrix)
Zhang, J., Duan, R., Tian, Y., & Konno, K. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2009.02.053 · Cited by 82 · see citing works
Water and Carbon Dioxide: Green Solvents for the Extraction of Collagen/Gelatin from Marine Sponges
Barros, A. A., Aroso, I. M., Silva, T. H., et al. (2014) · ACS Sustainable Chemistry & Engineering · doi:10.1021/sc500621z · Cited by 81 · see citing works
Fiorani, A., Gualandi, C., Panseri, S., Montesi, M., Marcacci, M., Focarete, M. L., & Bigi, A. (2014) · Journal of Materials Science Materials in Medicine · doi:10.1007/s10856-014-5196-2 · Cited by 78 · see citing works
Effects of solar radiation on collagen and chitosan films
Sionkowska, A. (2005) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2005.08.003 · Cited by 78 · see citing works
Metreveli, N., Jariashvili, K., Namicheishvili, L., Svintradze, D. V., Chikvaidze, E. N., Sionkowska, A., & Skopińska-Wiśniewska, J. (2009) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2009.12.005 · Cited by 77 · see citing works
Akkouch, A., Zhang, Z., & Rouabhia, M. (2014) · Journal of Biomaterials Applications · doi:10.1177/0885328213486705 · Cited by 76 · cited 1× · see citing works
“(169) design a new natural/synthetic bioactive bone scaffold for potential use in bone replacement application.”
BackgroundStudy on the stabilisation of collagen with vegetable tannins in the presence of acrylic polymer
Madhan, B., Muralidharan, C., & Jayakumar, R. (2002) · Biomaterials · doi:10.1016/s0142-9612(01)00410-0 · Cited by 76 · see citing works
Identification and Characterization of Molecular Species of Collagen in Fish Skin
Yata, M., Yoshida, C., Fujisawa, S., et al. (2001) · Journal of Food Science · doi:10.1111/j.1365-2621.2001.tb11325.x · Cited by 73 · see citing works
Elango, J., Wu, W., Nan-ping, W., et al. (2014) · Process Biochemistry · doi:10.1016/j.procbio.2014.06.011 · Cited by 72 · see citing works
Zeng, S., Yin, J., Yang, S., et al. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2012.06.086 · Cited by 72 · see citing works
Liu, X., Dan, N., & Dan, W. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.03.066 · Cited by 71 · see citing works
Coelho, R. C. G., Marques, A. L. P., Oliveira, S. M., et al. (2017) · Materials Science and Engineering C · doi:10.1016/j.msec.2017.04.122 · Cited by 69 · see citing works
Synthetic collagen fascicles for the regeneration of tendon tissue
Kew, S. J., Gwynne, J. H., Enea, D., et al. (2012) · Acta Biomaterialia · doi:10.1016/j.actbio.2012.06.018 · Cited by 68 · see citing works
Tylingo, R., & Mania, S. (2016) · Journal of Biotechnology & Biomaterials · doi:10.4172/2155-952x.1000234 · Cited by 66 · see citing works
Wu, J., Zheng, Y., Yang, Z., et al. (2013) · RSC Advances · doi:10.1039/c3ra45407j · Cited by 64 · see citing works
Krishnamoorthi, J., Ramasamy, P., Shanmugam, V., & Shanmugam, A. (2017) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2017.02.006 · Cited by 64 · see citing works
Modification of carboxymethyl cellulose grafted with collagen peptide and its antioxidant activity
Fan, L., Peng, M., Zhou, X., et al. (2014) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2014.05.056 · Cited by 62 · see citing works
Isolation and characterization of collagen from the skin of Brama australis
Sionkowska, A., Kozłowska, J., Skorupska, M., & Michalska, M. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.07.032 · Cited by 60 · see citing works
Ma, X., Deng, J., Du, Y., Li, X., Fan, D., Zhu, C., Hui, J., Ma, P., & Xue, W. (2014) · Journal of Materials Chemistry B · doi:10.1039/c3tb21842b · Cited by 59 · see citing works
Nagiah, N., Madhavi, L., Anitha, R., et al. (2013) · Polymer Bulletin · doi:10.1007/s00289-013-0956-6 · Cited by 58 · see citing works
Characteristics of Pepsin‐Solubilised Collagen from the Skin of Splendid Squid ( Loligo formosana )
Kittiphattanabawon, P., Nalinanon, S., Benjakul, S., et al. (2015) · Journal of Chemistry · doi:10.1155/2015/482354 · Cited by 58 · see citing works
Kim, Z.-H., Lee, Y., Kim, S., Kim, H., Yun, C., & Choi, Y. (2015) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.1411.11029 · Cited by 58 · see citing works
Vigneswari, S., Murugaiyah, V., Kaur, G., et al. (2016) · Materials Science and Engineering C · doi:10.1016/j.msec.2016.03.102 · Cited by 58 · see citing works
Studies on fish scale collagen of Pacific saury (Cololabis saira)
Mori, H., Tone, Y., Shimizu, K., et al. (2012) · Materials Science and Engineering C · doi:10.1016/j.msec.2012.08.025 · Cited by 57 · see citing works
Zheng, Y., Wen, X., Wu, J., Wang, L., Yuan, Z., Peng, J., & Meng, H. (2015) · International Journal of Nanomedicine · doi:10.2147/ijn.s84452 · Cited by 56 · see citing works
Comparison of acid-soluble collagens from the skins and scales of four carp species
Liu, D., Zhou, P., Li, T., & Regenstein, J. M. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.04.030 · Cited by 56 · see citing works
Zhang, F., Qian, Y., Chen, H., Xu, Y., Yang, J., Zhou, X., & Gu, N. (2016) · International Journal of Nanomedicine · doi:10.2147/ijn.s110577 · Cited by 55 · see citing works
Biochemical properties of alligator (Alligator mississippiensis) bone collagen
Wood, A., Ogawa, M., Portier, R. J., Schexnayder, M., Shirley, M., & Losso, J. N. (2008) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2008.05.015 · Cited by 54 · see citing works
Hung, H., Chang, C.-H., Chang, C.-J., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0104019 · Cited by 54 · see citing works
Facing the challenge of biosample imaging by FTIR with a synchrotron radiation source
Petibois, C., Piccinini, M., Guidi, M. C., & Marcelli, A. (2009) · Journal of Synchrotron Radiation · doi:10.1107/s0909049509046056 · Cited by 51 · see citing works
Elango, J., Bu, Y., Bin, B., et al. (2016) · Food Bioscience · doi:10.1016/j.fbio.2016.12.002 · Cited by 51 · see citing works
Sangkert, S., Meesane, J., Kamonmattayakul, S., et al. (2015) · Materials Science and Engineering C · doi:10.1016/j.msec.2015.09.031 · Cited by 50 · see citing works
Sun, T., Zhu, Y., Chen, F., et al. (2017) · Chemistry - An Asian Journal · doi:10.1002/asia.201601592 · Cited by 50 · see citing works
Surface Chemistry of Nanoscale Mineralized Collagen Regulates Periodontal Ligament Stem Cell Fate
Fu, Y., Liu, S., Cui, S., et al. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b04951 · Cited by 49 · see citing works
Extraction and Characterization of Collagen from Buffalo Skin for Biomedical Applications
Rizk, M. A., & Mostafa, N. Y. (2016) · Oriental Journal Of Chemistry · doi:10.13005/ojc/320336 · Cited by 49 · see citing works
Nguyen, T. T., Eklouh‐Molinier, C., Sebiskveradze, D., et al. (2014) · The Analyst · doi:10.1039/c3an00353a · Cited by 48 · see citing works
Regulation of biodegradability and drug release behavior of aliphatic polyesters by blending
Shen, Y., Sun, W., Zhu, K. J., & Shen, Z. (2000) · Journal of Biomedical Materials Research · doi:10.1002/(sici)1097-4636(20000615)50:4 · Cited by 47 · see citing works
Long, T., Yang, J., Shi, S., et al. (2014) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.33328 · Cited by 46 · see citing works
Chen, F., Zhu, Y., Zhao, X., Lu, B., & Wu, J. L. (2013) · CrystEngComm · doi:10.1039/c3ce40115d · Cited by 45 · see citing works
Chen, L., Hu, J., Ran, J., Shen, X., & Tong, H. (2014) · Polymer Composites · doi:10.1002/pc.23157 · Cited by 45 · see citing works
Fabrication of duck’s feet collagen–silk hybrid biomaterial for tissue engineering
Kim, S. H., Park, H. S., Lee, O. J., Chao, J. R., Park, H.-J., Lee, J. M., Ju, H. W., Moon, B. M., Park, Y. R., Song, J. E., et al. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.12.086 · Cited by 45 · see citing works
Preparation, Cell Compatibility and Degradability of Collagen-Modified Poly(lactic acid)
Cui, M., Liu, L., Guo, N., et al. (2015) · Molecules · doi:10.3390/molecules20010595 · Cited by 43 · see citing works
Obtenção e caracterização de blendas colágeno-quitosana
Tonhi, E., & Plepis, A. M. D. G. (2002) · Química Nova · doi:10.1590/s0100-40422002000600011 · Cited by 42 · see citing works
Sadeghi-Avalshahr, A. R., Khorsand-Ghayeni, M., Nokhasteh, S., et al. (2016) · Journal of Materials Science Materials in Medicine · doi:10.1007/s10856-016-5789-z · Cited by 42 · see citing works
Drug release from collagen matrices including an evolving microstructure
Ray, N., van Noorden, T., Radu, F. A., et al. (2013) · ZAMM ‐ Journal of Applied Mathematics and Mechanics / Zeitschrift für Angewandte Mathematik und Mechanik · doi:10.1002/zamm.201200196 · Cited by 40 · see citing works
Tang, Z. G., & Hunt, J. A. (2006) · Biomaterials · doi:10.1016/j.biomaterials.2006.04.009 · Cited by 39 · see citing works
Begam, H., Nandi, S. K., Chanda, A., et al. (2017) · Research in Veterinary Science · doi:10.1016/j.rvsc.2017.01.012 · Cited by 39 · see citing works
Characterization of collagen from emu (Dromaius novaehollandiae) skins
Nagai, T., Tanoue, Y., Kai, N., et al. (2014) · Journal of Food Science and Technology · doi:10.1007/s13197-014-1266-1 · Cited by 37 · see citing works
Teebken, O. E., Puschmann, C., Breitenbach, I., et al. (2008) · European Journal of Vascular and Endovascular Surgery · doi:10.1016/j.ejvs.2008.10.012 · Cited by 36 · see citing works
Kanungo, I., Fathima, N. N., Rao, J. R., et al. (2013) · Materials Science and Engineering C · doi:10.1016/j.msec.2013.07.020 · Cited by 36 · see citing works
Ramanathan, G., Singaravelu, S., Raja, M. D., et al. (2014) · Journal of Biomaterials and Tissue Engineering · doi:10.1166/jbt.2014.1157 · Cited by 36 · see citing works
Prominent Vascularization Capacity of Mesenchymal Stem Cells in Collagen–Gold Nanocomposites
Hsieh, S., Chen, H.-J., Hsu, S., et al. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b09330 · Cited by 35 · see citing works
Mitra, T., Sailakshmi, G., & Gnanamani, A. (2014) · Journal of Chemical Sciences · doi:10.1007/s12039-013-0543-2 · Cited by 34 · see citing works
Pulsed laser deposition of collagen and keratin
Tsuboi, Y., Kimoto, N., Kabeshita, M., et al. (2001) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/s1010-6030(01)00584-6 · Cited by 33 · see citing works
Johnson, K. (1999) · Biomaterials · doi:10.1016/s0142-9612(98)90187-9 · Cited by 33 · see citing works
Biological Dressings in Burns—A Review
Peters, W. J. (1980) · Annals of Plastic Surgery · doi:10.1097/00000637-198002000-00010 · Cited by 31 · see citing works
Innovative Composite Films of Chitosan, Methylcellulose, and Nanoparticles
Mura, S., Corrias, F., Stara, G., et al. (2011) · Journal of Food Science · doi:10.1111/j.1750-3841.2011.02295.x · Cited by 31 · see citing works
Guilbert, M., Roig, B., Terryn, C., Garnotel, R., Jeannesson, P., Sockalingum, G. D., Manfait, M., Perraut, F., Dinten, J., Koenig, A., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7385 · Cited by 30 · see citing works
Characterization of Acid-soluble Collagen from the Skin of Hammerhead Shark (Sphyrna lewini )
Chi, C., Wang, B., Li, Z., et al. (2013) · Journal of Food Biochemistry · doi:10.1111/jfbc.12042 · Cited by 28 · see citing works
Pietrucha, K., Marzec, E., & Kudzin, M. H. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.08.029 · Cited by 28 · see citing works
Comparison of collagen characteristics of sea- and freshwater-rainbow trout skin
Lee, J. K., Kang, S. I., Kim, Y. J., et al. (2016) · Food Science and Biotechnology · doi:10.1007/s10068-016-0020-z · Cited by 27 · see citing works
In vitro collagen fibril alignment via incorporation of nanocrystalline cellulose
Rudisill, S. G., DiVito, M. D., Hubel, A., et al. (2014) · Acta Biomaterialia · doi:10.1016/j.actbio.2014.10.024 · Cited by 26 · see citing works
The mechanical property of Rana chensinensis skin collagen/poly(L-lactide) fibrous membrane
Zhang, M., Wang, J., Xu, W., Luan, J., Li, X., Zhang, Y., Dong, H., & Sun, D. (2014) · Materials Letters · doi:10.1016/j.matlet.2014.10.085 · Cited by 25 · see citing works
Niflumic acid-collagen delivery systems used as anti-inflammatory drugs and analgesics in dentistry
Barbaresso, R. C., Rau, I. B., Zgârian, R. G., et al. (2013) · Comptes Rendus Chimie · doi:10.1016/j.crci.2013.07.007 · Cited by 25 · see citing works
Huang, Y., Niu, X., Wang, L., Fan, J., Li, X., Zhou, G., Feng, Q., & Fan, Y. (2013) · Journal of Composite Materials · doi:10.1177/0021998313493808 · Cited by 19 · see citing works
Zhang, M., Li, Z., Jiang, P., Lin, T., Li, X., & Sun, D. (2017) · Journal of Applied Polymer Science · doi:10.1002/app.45109 · Cited by 19 · see citing works
Effects of solar radiation on collagen‐based biomaterials
Sionkowska, A., Wiśniewski, M., Skopińska-Wiśniewska, J., et al. (2006) · International Journal of Photoenergy · doi:10.1155/ijp/2006/29196 · Cited by 18 · see citing works
Wu, C.-S. (2014) · Materials Science and Engineering C · doi:10.1016/j.msec.2014.12.013 · Cited by 18 · see citing works
A Case of Complication after Matridex® Injection
Huh, S. Y., Cho, S., Kim, K. H., et al. (2010) · Annals of Dermatology · doi:10.5021/ad.2010.22.1.81 · Cited by 17 · see citing works
Shin, K.-H., Sung, J.-H., Koh, Y., Lee, J., Choi, W.-Y., & Kim, H. (2010) · Materials Letters · doi:10.1016/j.matlet.2010.04.014 · Cited by 16 · see citing works
Stabilization of collagen by cross-linking with oxazolidine E-resorcinol
Chen, H., & Shana, Z.-H. (2010) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2010.03.001 · Cited by 16 · see citing works
The influence of methylene blue on the photochemical stability of collagen
Sionkowska, A. (2000) · Polymer Degradation and Stability · doi:10.1016/s0141-3910(99)00084-1 · Cited by 15 · see citing works
siRNA and miRNA gene silencing : from bench to bedside
Sioud, M. (2009) · Cited by 9 · see citing works
Park, K.-H., Kim, S. W., & Bae, Y. H. (2001) · Journal of Biomedical Materials Research · doi:10.1002/1097-4636(200104)55:1 · Cited by 9 · see citing works
Modification of chrome tanned leather waste hydrolysate with epichlorhydrin
Langmaier, F., Karnas, R., & Mokrejš, P. (2006) · Repository of TBU publications (Univerzita Tomase Bati ze Zline) · Cited by 8 · see citing works
Effect of UV on stability of collagen with consideration of hydratation and fibrillogenesis
Xing, J., Bai, B., Xue, W., et al. (2013) · Food Science and Biotechnology · doi:10.1007/s10068-013-0204-8 · Cited by 7 · see citing works
Wang, T., Li, Q., Zhang, G., Zhou, G., Yu, X., Zhang, J., Wang, X., & Tang, Z. (2016) · Frontiers of Materials Science · doi:10.1007/s11706-016-0333-0 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Phytobioactive compounds as therapeutic agents for human diseases: A review
Riaz, M., Khalid, R., Afzal, M., Anjum, F., Fatima, H., Zia, S., Rasool, G., Egbuna, C., Mtewa, A. G., Uche, C. Z., et al. (2023) · Food Science & Nutrition · doi:10.1002/fsn3.3308 · Cited by 355 · see citing works
Jeong, W., Kim, M. K., & Kang, H.-W. (2021) · Journal of Tissue Engineering · doi:10.1177/2041731421997091 · Cited by 53 · see citing works
Sun, Y., Chai, X., Han, W., Farah, Z., Tian, T., Xu, Y.-J., & Liu, Y. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108434 · Cited by 34 · see citing works
Yang, M., Yu, S., Zhao, P., Shi, G., Guo, Y., Xie, L., Lyu, G., & Yu, J. (2023) · International Wound Journal · doi:10.1111/iwj.13910 · Cited by 13 · see citing works
Antunes, B. S. L., Pedrini, F., Komatsu, D., Asami, J., Dicko, C., & Duek, E. A. R. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154129
- Authors
- Riaz, T., Zeeshan, R., Zarif, F., Ilyas, K., Muhammad, N., Safi, S. Z., Rahim, A., Rizvi, S. A. A., & Rehman, I. U.
- Affiliations
- COMSATS University Islamabad, Lahore Campus (PK)
- Nova Southeastern University (US)
- University of Sheffield (GB)
- Corresponding author
- Muhammad, Nawshad
- Rehman, Ihtesham Ur
- Venue
- Applied Spectroscopy Reviews
- Publisher
- Informa UK Limited
- Published
- 2018-03
- Volume
- 53
- Issue
- 9
- Pages
- 703-746
- ISSN
- 0570-4928 (ISSN-L)
- 1520-569X
- OpenAlex
- W2792517670
- Cited by
- 628
- References
- 170
- Citations by year
- 2026: 84 · 2025: 111 · 2024: 116 · 2023: 89 · 2022: 71 · 2021: 77 · 2020: 58 · 2019: 19 · 2018: 2
- FWCI
- 12.64
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Applied Spectroscopy Reviews (publishedVersion)
- Lancaster EPrints (Lancaster University) (submittedVersion)
- Funders
- Interdisciplinary Research Centre in Biomedical Materials (IRCBM) COMSATS Institute of Information Technology
- Higher Education Commission of Pakistan (N0.20-4146/R&D/HEC/14)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Spectroscopy Techniques in Biomedical and Chemical Research
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Keywords
- collagen, FTIR spectroscopy, collagen-based biomaterials, wound healing, skin substitutes, dermal fillers, skin aging, tissue engineering, bone regeneration, osteogenic differentiation, dental applications, cleft palate, alveolar ridge preservation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review