Therapeutic peptides: Historical perspectives, current development trends, and future directions

A new antibiotic kills pathogens without detectable resistance

Ling, L. L., Schneider, T., Peoples, A. J., Spoering, A. L., Engels, I., Conlon, B. P., Müller, A., Schäberle, T. F., Hughes, D. E., Epstein, S. S., et al. (2015) · Nature · doi:10.1038/nature14098 · Cited by 2,428

American Association of Clinical Endocrinologists and American College of Endocrinology Clinical Practice Guidelines for the Diagnosis and Treatment of Postmenopausal Osteoporosis — 2016--Executive Summary

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Cilengitide combined with standard treatment for patients with newly diagnosed glioblastoma with methylated MGMT promoter (CENTRIC EORTC 26071-22072 study): a multicentre, randomised, open-label, phase 3 trial

Stupp, R., Hegi, M. E., Gorlia, T., Erridge, S. C., Perry, J., Hong, Y.-K., Aldape, K. D., Lhermitte, B., Pietsch, T., Grujicic, D., et al. (2014) · The Lancet Oncology · doi:10.1016/s1470-2045(14)70379-1 · Cited by 1,052

Advances in Fmoc solid‐phase peptide synthesis

Behrendt, R., White, P., & Offer, J. (2016) · Journal of Peptide Science · doi:10.1002/psc.2836 · Cited by 767

Untitled work

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Unimolecular Dual Incretins Maximize Metabolic Benefits in Rodents, Monkeys, and Humans

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Stapled α−helical peptide drug development: A potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy

Chang, Y. S., Graves, B. J., Guerlavais, V., Tovar, C., Packman, K. E., To, K.-H., Olson, K. A., Kesavan, K. P., Gangurde, P., Mukherjee, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303002110 · Cited by 681

Strategic Approaches to Optimizing Peptide ADME Properties

Di, L. (2015) · The AAPS Journal · doi:10.1208/s12248-014-9687-3 · Cited by 669

Large-scale manufacture of peptide therapeutics by chemical synthesis

Bray, B. L. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1133 · Cited by 601

Asprosin, a Fasting-Induced Glucogenic Protein Hormone

Romere, C., Duerrschmid, C., Bournat, J., Constable, P., Jain, M., Xia, F., Saha, P. K., Del Solar, M., Zhu, B., York, B., et al. (2016) · Cell · doi:10.1016/j.cell.2016.02.063 · Cited by 591

Green solvent mixture for ultrasound-assisted solid-phase peptide synthesis: a fast and versatile method and its applications in flow and natural product synthesis

Liao, J., Zhang, R., Jia, X., Wang, M., Li, C., Wang, J., Tang, R., Huang, J., You, H., & Chen, F. (2024) · Green Chemistry · doi:10.1039/d4gc03864a · Cited by 13

Different Strategies for the Biosynthesis of Bioactive Peptide Using Bioengineering Technology in Pichia pastoris: A Review

Hong, K., Rong, Y., Jiang, Y., Yuan, J., Wu, F., Gao, L., & Wu, X. (2025) · Food and Bioprocess Technology · doi:10.1007/s11947-025-03755-3 · Cited by 16

Peptide classification landscape: An in-depth systematic literature review on peptide types, databases, datasets, predictors architectures and performance

Asim, M. N., Asif, T., Mehmood, F., & Dengel, A. R. (2025) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2025.109821 · Cited by 14

Recent Advances in the Addition of Amide/Sulfonamide Bonds to Alkynes

Zhao, F., Li, P., Liu, X., Jia, X., Wang, J., & Liu, H. S. (2019) · Molecules · doi:10.3390/molecules24010164 · Cited by 13

Diversity-oriented submonomer synthesis of azapeptides mediated by the Mitsunobu reaction

Dai, C., Ma, J., Li, M., Wu, W., Xia, X., & Zhang, J. (2019) · Organic Chemistry Frontiers · doi:10.1039/c9qo00296k · Cited by 13

Synthesis, X-ray crystal structure, Hirshfeld surface analysis, and molecular docking study of novel inhibitor of hepatitis B: methyl 4-fluoro-3-(morpholinosulfonyl)benzo[b]thiophene-2-carboxylate

Ivachtchenko, A. V., Mitkin, O. D., Kravchenko, D. V., Kovalenko, S. М., Shishkina, S. V., Bunyatyan, N. D., Konovalova, I. S., Геннадиевна, Д. И., Ivanov, V. V., & Langer, T. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e02738 · Cited by 13

Antifungal and anti-biofilm activity of designed derivatives from kyotorphin

de Andrade, V. M., Bardajı́, E., Heras, M., Ramu, V. G., Junqueira, J. C., dos Santos, J. D., Castanho, M. A. R. B., & Conceição, K. (2019) · Fungal Biology · doi:10.1016/j.funbio.2019.12.002 · Cited by 13

Peptide Combination Generator: a Tool for Generating Peptide Combinations

Ali, N., Shamoon, A., Yadav, N., & Sharma, T. (2020) · ACS Omega · doi:10.1021/acsomega.9b03848 · Cited by 13

Evolving peptides for oral intake

Brayden, D. J. (2020) · Nature Biomedical Engineering · doi:10.1038/s41551-020-0559-0 · Cited by 13

Can cheese mites, maggots and molds enhance bioactivity? Peptidomic investigation of functional peptides in four traditional cheeses

Robinson, R. C., Nielsen, S. D.-H., Dallas, D. C., & Barile, D. (2020) · Food & Function · doi:10.1039/d0fo02439b · Cited by 15

Fluorinated Triazole Foldamers: Folded or Extended Conformational Preferences

Arenas, J. L., Xu, Y., Milcent, T., van Heijenoort, C., Giraud, F., Ha‐Duong, T., Crousse, B., & Ongeri, S. (2021) · ChemPlusChem · doi:10.1002/cplu.202000791 · Cited by 13

Complexation of exenatide and cyclodextrin: An approach for the stabilization and sustained release of exenatide in PLGA microsphere

Park, H., Ha, E., & Kim, M. (2021) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2021.118169 · Cited by 13

Decarboxylative Radical Addition to Methylideneoxazolidinones for Stereocontrolled Synthesis of Selectively Protected Diamino Diacids

Hsiao, Y., Beadle, J. D., Pascoe, C. A., Annadate, R. A., & Vederas, J. C. (2021) · Organic Letters · doi:10.1021/acs.orglett.1c02684 · Cited by 13

Rational design and synthesis of modified natural peptides from Boana pulchella (anura) as acetylcholinesterase inhibitors and antioxidants

Sanchís, I., Spinelli, R., Aschemacher, N. A., & Siano, Á. (2021) · Amino Acids · doi:10.1007/s00726-021-03096-3 · Cited by 13

Penta-peptide ATN-161 based neutralization mechanism of SARS-CoV-2 spike protein

Rabbani, G., Ahn, S. N., Kwon, H., Ahmad, K., & Choi, I. (2021) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2021.101170 · Cited by 13

Development of Peptide Biopharmaceuticals in Russia

Deigin, V. I., Poluektova, E. A., Герович, Б. А., Kozin, S. A., & Poluektov, Y. M. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14040716 · Cited by 13

General lack of structural characterization of chemically synthesized long peptides

Boutin, J. A., Tartar, A. L., DORSSELAER, A. V., & Vaudry, H. (2019) · Protein Science · doi:10.1002/pro.3601 · Cited by 13

Quantitative sequence-activity modeling of ACE peptide originated from milk using ACC–QTMS amino acid indices

Bahadori, M., Hemmateenejad, B., & Yousefinejad, S. (2019) · Amino Acids · doi:10.1007/s00726-019-02761-y · Cited by 13

Beyond function: Engineering improved peptides for therapeutic applications

Adhikari, S., Leissa, J. A., & Karlsson, A. J. (2019) · AIChE Journal · doi:10.1002/aic.16776 · Cited by 12

Estimation of a stronger heparin binding locus in fibronectin domain III 14 using thermodynamics and molecular dynamics

Gupta, S., Tiwari, N., Verma, J. K., Waseem, M., Subbarao, N., & Munde, M. M. (2020) · RSC Advances · doi:10.1039/d0ra01773f · Cited by 14

Isolation of Cysteine-Rich Peptides from Citrullus colocynthis

Shahin-Kaleybar, B., Niazi‎, A., Afsharifar, A., Nematzadeh, G., Yousefi, R., Retzl, B., Hellinger, R., Muratspahić, E., & Gruber, C. W. (2020) · Biomolecules · doi:10.3390/biom10091326 · Cited by 13

Antimicrobial Excipient-Induced Reversible Association of Therapeutic Peptides in Parenteral Formulations

D’Addio, S. M., Su, Y., Yin, D., Zhang, J., Kemp, E. A., & Gindy, M. E. (2020) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2020.09.027 · Cited by 13

Peptidomimetics Therapeutics for Retinal Disease

Parsons, D., Hyeon, L. S., Sun, Y. J., Velez, G., Bassuk, A. G., Smith, M. A., & Mahajan, V. B. (2021) · Biomolecules · doi:10.3390/biom11030339 · Cited by 13

Assessing sequence-based protein–protein interaction predictors for use in therapeutic peptide engineering

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Advancing the valorisation of meat co-products in food, pet food, and biomedicine applications

Bou, R., Pinotti, L., Zeugolis, D. I., Watigny, A., & Álvarez, C. (2025) · Waste Management · doi:10.1016/j.wasman.2025.114948 · Cited by 15

Backbone Protecting Groups for Enhanced Peptide and Protein Synthesis

Paravizzini, S. J., Haugaard‐Kedström, L. M., Hutton, C. A., & Karas, J. A. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202509939 · Cited by 12

Accurate structure prediction of cyclic peptides containing unnatural amino acids using HighFold3

Cao, S., Zhu, C., Mao, Q., Guo, J., Zhu, N., & Duan, H. (2025) · Briefings in Bioinformatics · doi:10.1093/bib/bbaf488 · Cited by 12

Potential therapeutic applications of AKAP disrupting peptides

Murabito, A., Cnudde, S., Hirsch, E., & Ghigo, A. (2020) · Clinical Science · doi:10.1042/cs20201244 · Cited by 12

An integrated platform approach enables discovery of potent, selective and ligand-competitive cyclic peptides targeting the GIP receptor

Bhushan, B., Granata, D., Kaas, C. S., Kasimova, M. A., Ren, Q., Cramer, C. N., White, M. D., Hansen, A. M. K., Fledelius, C., Invernizzi, G., et al. (2022) · Chemical Science · doi:10.1039/d1sc06844j · Cited by 13

Metabolic composition of the cyanobacterium Nostoc muscorum as a function of culture time: A 1H NMR metabolomics study

Maçario, I. P. E., Veloso, T., Romão, J., Gonçalves, F. J. M., Pereira, J. L., Duarte, I. F., & Ventura, S. P. M. (2022) · Algal Research · doi:10.1016/j.algal.2022.102792 · Cited by 13

Electrochemical Detection of Carcinoembryonic Antigen in Human Serum Based on Designed Anti-Fouling and Anti-Enzymolysis Peptides Conjugated with Silk Sericine-Inspired Beta-Homoserine

Zhao, S., Song, Z., Liu, T., Wang, X., Li, Y., Xu, Y., Wang, H., Wu, Y., & Luo, X. (2022) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2022.133166 · Cited by 12

Inhibition of GSDMD activation by Z-LLSD-FMK or Z-YVAD-FMK reduces vascular inflammation and atherosclerotic lesion development in ApoE−/− mice

Zhang, B., Yu, P., Su, E., Zhang, C.-Y., Xie, S., Yang, X., Zou, Y., Liu, M., & Jiang, H. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1184588 · Cited by 12

Pd(I)-catalyzed ring-opening arylation of cyclopropyl-α-aminoamides: Access to α-ketoamide peptidomimetics

Sun, Y., Yang, L., Cheng, Y., An, G., & Li, G. (2023) · Chinese Chemical Letters · doi:10.1016/j.cclet.2023.109250 · Cited by 13

EACVP: An ESM-2 LM Framework Combined CNN and CBAM Attention to Predict Anti-coronavirus Peptides

Zhang, S., Jing, Y., & Liang, Y. (2024) · Current Medicinal Chemistry · doi:10.2174/0109298673287899240303164403 · Cited by 12

Peptide Drugs: Current Status and it's Applications in the Treatment of Various Diseases

Chandarana, C. V., Juwarwala, I., Shetty, S., & Bose, A. (2024) · Current Drug Research Reviews · doi:10.2174/0125899775295960240406073630 · Cited by 12

Allenamides as a Powerful Tool to Incorporate Diversity: Thia‐Michael Lipidation of Semisynthetic Peptides and Access to β‐Keto Amides

Na, T., Sander, V., Davidson, A. J., Lin, R., Hermant, Y. O., Boys, M. T. H., Pletzer, D., Campbell, G., Ferguson, S. A., Cook, G. M., et al. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202407764 · Cited by 12

Local and Systemic Peptide Therapies for Soft Tissue Regeneration: A Narrative Review

Cushman, C. J., Ibrahim, A. F., Smith, A. D., Hernandez, E. J., MacKay, B., & Zumwalt, M. (2024) · The Yale Journal of Biology and Medicine · doi:10.59249/tknm3388 · Cited by 12

Direct and chemoselective transformation of cysteine to dehydroalanine on peptides

Mori, T., Sakata, K., & Shirakawa, S. (2025) · Chemical Communications · doi:10.1039/d5cc00156k · Cited by 12

Hepatic micropeptide modulates mitochondrial RNA processing machinery in hepatocellular carcinoma

Zhu, L., Liu, F., Shi, C., Su, X., Tan, M., Xie, S., Meng, Y., Zou, S., Tan, Y., Xie, S., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.05.027 · Cited by 13

Fluorescent and Photosensitizing Conjugates of Cell-Penetrating Peptide TAT(47-57): Design, Microwave-Assisted Synthesis at 60 °C, and Properties

Okuda-Shinagawa, N. M., Moskalenko, Y. E., Junqueira, H. C., Baptista, M. S., Marques, C. M., & de Miranda, M. T. M. (2017) · ACS Omega · doi:10.1021/acsomega.7b01127 · Cited by 12

Real-Time Imaging and Quantification of Peptide Uptake in Vitro and in Vivo

Karataş, H., Maric, T., D’Alessandro, P. L., Yevtodiyenko, A., Vorherr, T. E., Hollingworth, G. J., & Goun, E. A. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00439 · Cited by 12

Unwanted hydrolysis or α/β-peptide bond formation: how long should the rate-limiting coupling step take?

Gőz, V. G., Nagy, A., Farkas, V., Keszei, E., & Perczel, A. (2019) · RSC Advances · doi:10.1039/c9ra06124j · Cited by 12

Complex injectables

Pandey, A. P., Singh, D., Dhas, N. L., Tewari, A. K., Pathak, K., Chatap, V. K., Rathore, K. S., & Mutalik, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-817776-1.00008-0 · Cited by 12

Structure-based design of small bicyclic peptide inhibitors of Cripto-1 activity

Iaccarino, E., Calvanese, L., Untiveros, G., Falcigno, L., D’Auria, G., Latino, D., Sivaccumar, J. P., Strizzi, L., Ruvo, M., & Sandomenico, A. (2020) · Biochemical Journal · doi:10.1042/bcj20190953 · Cited by 12

Effects of Single α-to-β Residue Replacements on Recognition of an Extended Segment in a Viral Fusion Protein

Outlaw, V. K., Kreitler, D. F., Stelitano, D., Porotto, M., Moscona, A., & Gellman, S. H. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00385 · Cited by 12

Targeting signal pathways triggered by cyclic peptides in cancer: Current trends and future challenges

Yang, Y., Mao, H. Z., Chen, L., & Li, L. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108776 · Cited by 12

An Optimized Protocol for the Synthesis of Peptides Containing trans‐Cyclooctene and Bicyclononyne Dienophiles as Useful Multifunctional Bioorthogonal Probes

La‐Venia, A., Dzijak, R., Rampmaier, R., & Vrábel, M. (2021) · Chemistry - A European Journal · doi:10.1002/chem.202102042 · Cited by 12

Nγ‐Hydroxyasparagine: A Multifunctional Unnatural Amino Acid That is a Good P1 Substrate of Asparaginyl Peptide Ligases

Xia, Y., To, J., Chan, N., Hu, S., Liew, H. T., Balamkundu, S., Zhang, X., Lescar, J., Bhattacharjya, S., Tam, J. P., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202108125 · Cited by 12

Peptide Blocking Self-Polymerization of Extracellular Calcium-Sensing Receptor Attenuates Hypoxia-Induced Pulmonary Hypertension

Xiao, R., Luo, S., Zhang, T., Lv, Y.-K., Wang, T., Zhang, J., Yuan, S., Ruiz, M., Dupuis, J., Zhu, L., et al. (2021) · Hypertension · doi:10.1161/hypertensionaha.120.16712 · Cited by 12

Deciphering the Limitations and Antibacterial Mechanism of Cruzioseptins

Rivera, F. V., Bermúdez-Puga, S., Proaño‐Bolaños, C., & Almeida, J. R. (2022) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-022-10383-4 · Cited by 12

Solid‐Phase Total Synthesis of Yaku'amide B Enabled by Traceless Staudinger Ligation

Itoh, H., Miura, K., Kamiya, K., Yamashita, T., & Inoue, M. (2020) · Angewandte Chemie · doi:10.1002/ange.201916517 · Cited by 12

Targeting NOX2 via p47/phox-p22/phox Inhibition with Novel Triproline Mimetics

Garsi, J.-B., Komjáti, B., Cullia, G., Fejes, I., Sipos, M., Sipos, Z., Fördős, E., Markacz, P., Balázs, B., Lancelot, N., et al. (2022) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.2c00094 · Cited by 13

Tuning of Peptide Cytotoxicity with Cell Penetrating Motif Activatable by Matrix Metalloproteinase-2

Lee, J., Oh, E., Lee, H., Lee, E., Kim, H. G., Park, H. J., & Kim, C. (2022) · ACS Omega · doi:10.1021/acsomega.2c02127 · Cited by 12

Synthetic amino acids-derived peptides target Cryptococcus neoformans by inducing cell membrane disruption

Sharma, K., Aaghaz, S., Maurya, I. K., Sharma, K. K., Singh, S., Rudramurthy, S. M., Kumar, V., Tikoo, K., & Jain, R. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106252 · Cited by 12

Targeting enteric release of therapeutic peptides by encapsulation in complex coacervated matrix microparticles by spray drying

Tang, Y., Arbaugh, B. M., Park, H., Scher, H. B., Bai, L., Mao, L., & Jeoh, T. (2022) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2022.104063 · Cited by 12

Late‐Stage, Stereoretentive, and Site‐Selective Modification of Synthetic Peptides by Using Photoredox Catalysis

Flitcroft, C. E., Jolliffe, K. A., & McErlean, C. S. P. (2023) · Chemistry - A European Journal · doi:10.1002/chem.202301083 · Cited by 12

DeepTPpred: A Deep Learning Approach With Matrix Factorization for Predicting Therapeutic Peptides by Integrating Length Information

Cui, Z. Y., Wang, S., He, Y., Chen, Z., & Zhang, Q. (2023) · IEEE Journal of Biomedical and Health Informatics · doi:10.1109/jbhi.2023.3290014 · Cited by 12

Covalent Macrocyclic Proteasome Inhibitors Mitigate Resistance in Plasmodium falciparum

Bennett, J. M., Ward, K. E., Muir, R. K., Kabeche, S. C., Yoo, E., Yeo, T., Lam, G., Zhang, H., Almaliti, J., Berger, G., et al. (2023) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.3c00310 · Cited by 12

Synthesis of the Antimalarial Peptide Aldehyde, a Precursor of Kozupeptin A, Utilizing a Designed Hydrophobic Anchor Molecule

Hayashi, Y., Hirose, T., Iwatsuki, M., Ōmura, S., & Sunazuka, T. (2019) · Organic Letters · doi:10.1021/acs.orglett.9b02966 · Cited by 12

Naturally occurring antitubercular cyclic peptides

Zhang, S., Kavianinia, I., & Brimble, M. A. (2019) · Tetrahedron Letters · doi:10.1016/j.tetlet.2019.151339 · Cited by 12

Mechanisms Inspired Targeting Peptides

Yuan, Y. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-3266-5_21 · Cited by 12

Increase in Toxicity of Anticancer Drugs by PMTPV, a Claudin-1-Binding Peptide, Mediated via Down-Regulation of Claudin-1 in Human Lung Adenocarcinoma A549 Cells

Nasako, H., Takashina, Y., Eguchi, H., Ito, A., Ishikawa, Y., Matsunaga, T., Endo, S., & Ikari, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165909 · Cited by 12

Bioresorbable Bone Graft Composed of an RGD-Enriched Recombinant Human Collagen Polypeptide Induced Neovascularization and Regeneration of Mature Bone Tissue

Hiratsuka, T., Ogura, I., Okamura, A., Fushimi, H., Yamaguchi, K., & Nishimura, I. (2020) · ACS Applied Bio Materials · doi:10.1021/acsabm.0c00986 · Cited by 12

Conventional Nanosized Drug Delivery Systems for Cancer Applications

Vergallo, C., Hafeez, M. N., Iannotta, D., Santos, H. A., d’Avanzo, N., Dini, L., Cilurzo, F., Fresta, M., Marzio, L. D., & Christian, C. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-58174-9_1 · Cited by 12

Peptide-Based Antiviral Drugs

Murugan, N. A., Raja, K. M. P., & Saraswathi, N. T. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-0267-2_10 · Cited by 12

Synthesis and conformation of backbone N-aminated peptides

Rathman, B. M., Rowe, J. L., & Valle, J. R. D. (2021) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2021.04.013 · Cited by 12

Advances of research of Fc-fusion protein that activate NK cells for tumor immunotherapy

Niu, Y.-X., Xu, Z., Yu, L., Lu, Y., Wang, Y., Wu, C., Hou, Y.-B., Li, J., Huang, S., Song, X., et al. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.108783 · Cited by 12

Looking for SARS-CoV-2 Therapeutics Through Computational Approaches

Vincenzi, M., Mercurio, F. A., & Leone, M. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666221004104430 · Cited by 13

The Importance of Amide Protons in Peptide Drug Development

Harrington, A., & Tal‐Gan, Y. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0238 · Cited by 12

Breaking the cellular delivery bottleneck: recent developments in direct cytosolic delivery of biologics

Nagaraj, H., Lehot, V., Nasim, N., Çiçek, Y. A., Goswami, R., Jeon, T., & Rotello, V. M. (2025) · RSC Pharmaceutics · doi:10.1039/d5pm00129c · Cited by 12

Thermodynamically stable colloid dispersion electrolytes with the Tyndall effect for practical zinc-ion pouch cells

Liu, Y., Meng, J., Yue, M., Jiao, C., Zhao, Z., Sun, Y., Chang, Y., Wu, H., Yan, X., Song, K., et al. (2025) · Energy & Environmental Science · doi:10.1039/d5ee05434f · Cited by 11

The Design and Optimization of Monomeric Multitarget Peptides for the Treatment of Multifactorial Diseases

Chen, T., Sun, T., Bian, Y., Pei, Y., Feng, F., Chi, H., Li, Y., Tang, X., Sang, S., Du, C., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01456 · Cited by 11

Subcutaneous catabolism of peptide therapeutics: bioanalytical approaches and ADME considerations

Esposito, S., Orsatti, L., & Pucci, V. (2022) · Xenobiotica · doi:10.1080/00498254.2022.2119180 · Cited by 11

Anti-Melanogenesis Effects of a Cyclic Peptide Derived from Flaxseed via Inhibition of CREB Pathway

Yoon, J. H., Jang, W. Y., Park, S. H., Kim, H. G., Shim, Y. Y., Reaney, M. J. T., & Cho, J. Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010536 · Cited by 13

Super silyl-based stable protecting groups for both the C- and N-terminals of peptides: applied as effective hydrophobic tags in liquid-phase peptide synthesis

Wu, A., & Yamamoto, H. (2023) · Chemical Science · doi:10.1039/d3sc01239e · Cited by 11

Computational analysis of spike protein of SARS-CoV-2 (Omicron variant) for development of peptide-based therapeutics and diagnostics

Pritam, M., Dutta, S., Medicherla, K. M., Kumar, R., & Singh, S. P. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2239932 · Cited by 11

A review on microneedle patch as a delivery system for proteins/peptides and their applications in transdermal inflammation suppression

Balde, A., Kim, S., & Nazeer, R. A. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.141963 · Cited by 11

Permeation Enhancer‐based Ionogel Shows Remarkable Potential for Oral Insulin Delivery

Raptis, K., Heade, J., da Cunha, C. F. B., van de Weert, M., Saaby, L., Rønholt, S., & Nielsen, H. M. (2025) · Advanced Healthcare Materials · doi:10.1002/adhm.202500946 · Cited by 11

De novo design of D-peptide ligands: Application to influenza virus hemagglutinin

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