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

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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

(1922) · PubMed · Cited by 753

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

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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

Overcoming Challenges in the Metabolism of Peptide Therapeutics: Strategies and Case Studies for Clinical Success

Ma, B., Fuhrmann, J., Henriksen, H. C., Khojasteh, S. C., Li, W., Liu, J., Plise, E. G., Yu, Q., & Cheruzel, L. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02276 · Cited by 30

Biomedical applications of radioiodinated peptides

Oliveira, M. C., & Correia, J. D. G. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.06.014 · Cited by 26

Furan-Conjugated Tripeptides as Potent Antitumor Drugs

Ali, H., Jabeen, A., Maharjan, R., Nadeem-Ul-Haque, M., Aamra, H., Nazir, S., Khan, S., Olleik, H., Maresca, M., & Shaheen, F. (2020) · Biomolecules · doi:10.3390/biom10121684 · Cited by 26

The allosteric modulation of complement C5 by knob domain peptides

Macpherson, A., Laabei, M., Ahdash, Z., Graewert, M. A., Birtley, J. R., Schulze, M. E. D., Crennell, S. J., Robinson, S. A., Holmes, B., Oleinikovas, V., et al. (2021) · eLife · doi:10.7554/elife.63586 · Cited by 24

A Review on the Metabolism of 25 Peptide Drugs

Chia, C. S. B. (2021) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-021-10177-0 · Cited by 26

Target-templated de novo design of macrocyclic d -/ l -peptides: discovery of drug-like inhibitors of PD-1

Guardiola, S., Varese, M., Roig, X., Sánchez‐Navarro, M., García, J., & Giralt, E. (2021) · Chemical Science · doi:10.1039/d1sc01031j · Cited by 25

Bioactive Synthetic Peptides for Oral Tissues Regeneration

Bermúdez, M., Hoz, L., Montoya, G. A., Campos, M. N., Pérez‐Soria, A., Romo, E., Soto‐Barreras, U., Garnica-Palazuelos, J. C., Aguilar‐Medina, M., Ramos‐Payán, R., et al. (2021) · Frontiers in Materials · doi:10.3389/fmats.2021.655495 · Cited by 26

Self-Assembly of an Antitumor Dipeptide Induced Near-Infrared Fluorescence and Improved Stability for Theranostic Applications

Lin, W., Yang, Y., Yang, L., An, F., Sun, L., Qin, Y. H., & Zhang, L. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c07983 · Cited by 26

A novel and low-toxic peptide DR3penA alleviates pulmonary fibrosis by regulating the MAPK/miR-23b-5p/AQP5 signaling axis

Wang, D., Deng, B., Cheng, L., Li, J., Zhang, J., Zhang, X., Guo, X., Yan, T., Xin, Y., An, Y., et al. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.09.001 · Cited by 25

HelixGAN a deep-learning methodology for conditional de novo design of α-helix structures

Xie, X., Valiente, P. A., & Kim, P. M. (2023) · Bioinformatics · doi:10.1093/bioinformatics/btad036 · Cited by 26

N‐Terminal‐Specific Dual Modification of Peptides through Copper‐Catalyzed [3+2] Cycloaddition

Machida, H., & Kanemoto, K. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202320012 · Cited by 27

Assessing the effectiveness of AS-48 in experimental mice models of Chagas’ disease

Martín‐Escolano, R., Cebrián, R., Maqueda, M., Romero, D., Rosales, M. J., Sánchez‐Moreno, M., & Marı́n, C. (2020) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkaa030 · Cited by 26

Concept for a Unidirectional Release Mucoadhesive Buccal Tablet for Oral Delivery of Antidiabetic Peptide Drugs Such as Insulin, Glucagon-like Peptide 1 (GLP-1), and their Analogs

Singh, A. P., Guo, Y., Baldelli, A., & Singh, A. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15092265 · Cited by 28

Review on therapeutic potential of peptides: Advancements in synthesis methods, linear and cyclic peptides, and strategies for overcoming challenges

Lalani, N., Tivari, S. R., Jain, V. D., & Jadeja, Y. S. (2024) · Peptide Science · doi:10.1002/pep2.24343 · Cited by 25

Developing Biologics Tablets: The Effects of Compression on the Structure and Stability of Bovine Serum Albumin and Lysozyme

Wei, Y., Wang, C., Jiang, B., Sun, C. C., & Middaugh, C. R. (2019) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.8b01118 · Cited by 25

Synthesis of secondary and tertiary amides without coupling agents from amines and potassium acyltrifluoroborates (KATs)

Schuhmacher, A., Shiro, T., Ryan, S. J., & Bode, J. W. (2020) · Chemical Science · doi:10.1039/d0sc01330g · Cited by 25

Cell-penetrating peptides containing 2,5-diketopiperazine (DKP) scaffolds as shuttles for anti-cancer drugs: conformational studies and biological activity

Feni, L., Jütten, L., Parente, S., Piarulli, U., Neundorf, I., & Díaz, D. (2020) · Chemical Communications · doi:10.1039/d0cc01490g · Cited by 25

An antitumor peptide RS17‐targeted CD47, design, synthesis, and antitumor activity

Wang, X., Wang, Y., Hu, J., & Xu, H. (2021) · Cancer Medicine · doi:10.1002/cam4.3768 · Cited by 25

Topical and nutricosmetic products for healthy hair and dermal antiaging using “dual‐acting” (2 for 1) plant‐based peptides, hormones, and cannabinoids

Sadgrove, N. J., & Simmonds, M. S. J. (2021) · FASEB BioAdvances · doi:10.1096/fba.2021-00022 · Cited by 26

Imaging therapeutic peptide transport across intestinal barriers

Larsen, J. B., Taebnia, N., Dolatshahi‐Pirouz, A., Eriksen, A. Z., Hjørringgaard, C. U., Kristensen, K., Larsen, N. W., Larsen, N. B., Marie, R., Mündler, A.-K., et al. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00024a · Cited by 26

Fatty Acid Modification of the Anticancer Peptide LVTX-9 to Enhance Its Cytotoxicity against Malignant Melanoma Cells

Li, F., Wu, S., Chen, N., Zhu, J., Zhao, X., Zhang, P., Zeng, Y., & Liu, Z. (2021) · Toxins · doi:10.3390/toxins13120867 · Cited by 26

Pan-RAS inhibitors: Hitting multiple RAS isozymes with one stone

Coley, A. B., Ward, A., Keeton, A. B., Chen, X., Maxuitenko, Y. Y., Prakash, A., Li, F., Foote, J. B., Buchsbaum, D. J., & Piazza, G. A. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.009 · Cited by 23

Oral delivery of glutathione: antioxidant function, barriers and strategies

Wei, T., Thakur, S. S., Liu, M., & Wen, J. (2022) · Acta Materia Medica · doi:10.15212/amm-2022-0005 · Cited by 27

Roles of Metal Ions in Foldamers and Other Conformationally Flexible Supramolecular Systems

Algar, J. L., Findlay, J. A., & Preston, D. (2022) · ACS Organic & Inorganic Au · doi:10.1021/acsorginorgau.2c00021 · Cited by 25

Efficient catalysis in dynamic nanomicelles of PS-750-M suspended in water

Kaur, G., Kaur, K., & Handa, S. (2022) · Current Opinion in Green and Sustainable Chemistry · doi:10.1016/j.cogsc.2022.100690 · Cited by 25

Alzheimer’s Disease: Challenges and a Therapeutic Opportunity to Treat It with a Neurotrophic Compound

Baazaoui, N., & Iqbal, K. (2022) · Biomolecules · doi:10.3390/biom12101409 · Cited by 27

A composite peptide-supramolecular microneedle system for melanoma immunotherapy

Li, M., Wang, M., Li, L., Zhang, L., Ma, B., & Wang, W. (2022) · Nano Research · doi:10.1007/s12274-022-5236-z · Cited by 25

Real‐Time Observation of Diarylethene‐Based Photoswitches in a Cyclic Peptide Environment

Schweigert, C., Babii, O., Afonin, S., Schober, T., Leier, J., Michenfelder, N. C., Komarov, I. V., Ulrich, A. S., & Unterreiner, A. (2019) · ChemPhotoChem · doi:10.1002/cptc.201900005 · Cited by 25

Modulation of the fate of zein nanoparticles by their coating with a Gantrez® AN-thiamine polymer conjugate

Inchaurraga, L., Martínez‐López, A. L., Abdulkarim, M., Gumbleton, M., Quincoces, G., Peñuelas, I., Martín‐Arbella, N., & Irache, J. M. (2019) · International Journal of Pharmaceutics X · doi:10.1016/j.ijpx.2019.100006 · Cited by 25

SARS-CoV-2 protein drug targets landscape: a potential pharmacological insight view for the new drug development

Chakraborty, C., Bhattacharya, M., Mallick, B., Sharma, A. R., Lee, S., & Agoramoorthy, G. (2021) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2021.1874348 · Cited by 25

Bioinspired Synthetic Peptide-Based Biomaterials Regenerate Bone through Biomimicking of Extracellular Matrix

Azadi, S., Yazdanpanah, M. A., Afshari, A., Alahdad, N., Chegeni, S., Angaji, A., Rezayat, S. M., & Tavakol, S. (2024) · Journal of Tissue Engineering · doi:10.1177/20417314241303818 · Cited by 24

A Comprehensive Overview of Antimicrobial Peptides: Broad-Spectrum Activity, Computational Approaches, and Applications

Marciano, C. L., de Lima, J. V. F., Rosa, M. S. D. C., do Nascimento, R. A., Ferraz, A. D. O., da Silva, I. C., Chrysostomo-Massaro, T. N., da Rosa-Garzon, N. G., & Cabral, H. (2025) · Antibiotics · doi:10.3390/antibiotics14111115 · Cited by 32

The disruption of protein-protein interactions as a therapeutic strategy for prostate cancer

Matos, B., Howl, J., Jerónimo, C., & Fardilha, M. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105145 · Cited by 26

Identification, heterologous production and bioactivity of lentinulin A and dendrothelin A, two natural variants of backbone N-methylated peptide macrocycle omphalotin A

Matabaro, E., Kaspar, H., Dahlin, P., Bader, D. L. V., Murar, C. E., Staubli, F., Field, C. M., Bode, J. W., & Künzler, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-83106-2 · Cited by 24

A Signaling View into the Inflammatory Tumor Microenvironment

Pereira, J., Jordan, P., & Matos, P. (2021) · Immuno · doi:10.3390/immuno1020007 · Cited by 24

MIF1 and MIF2 Myostatin Peptide Inhibitors as Potent Muscle Mass Regulators

Lee, E. J., Shaikh, S., Baig, M. H., Park, S., Lim, J. H., Ahmad, S. S., Ali, S. M., Ahmad, K., & Choi, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084222 · Cited by 24

Virtual Screening Expands the Non-Natural Amino Acid Palette for Peptide Optimization

Amarasinghe, K. N., Maria, L. D., Tyrchan, C., Eriksson, L. A., Sadowski, J., & Petrović, D. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c00193 · Cited by 24

In Silico Prediction of Anti-Infective and Cell-Penetrating Peptides from Thalassophryne nattereri Natterin Toxins

de Cena, G. L., Scavassa, B. V., & Conceição, K. (2022) · Pharmaceuticals · doi:10.3390/ph15091141 · Cited by 24

Handcrafted versus non-handcrafted (self-supervised) features for the classification of antimicrobial peptides: complementary or redundant?

García‐Jacas, C. R., García‐González, L. A., Martínez-Rios, F., Tapia-Contreras, I. P., & Brizuela, C. A. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac428 · Cited by 25

Peptides in Dentistry: A Scoping Review

Hardan, L., Chedid, J. C. A., Bourgi, R., Cuevas‐Suárez, C. E., Łukomska−Szymańska, M., Tosco, V., Avila, A. J. M., Jabra, M., Salloum-Yared, F., Kharouf, N., et al. (2023) · Bioengineering · doi:10.3390/bioengineering10020214 · Cited by 25

Eptifibatide, an Older Therapeutic Peptide with New Indications: From Clinical Pharmacology to Everyday Clinical Practice

Tonin, G., & Klen, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065446 · Cited by 24

Molecular Dynamics Simulation-Driven Focused Virtual Screening and Experimental Validation of Inhibitors for MTDH-SND1 Protein–Protein Interaction

Xu, Y.-D., Guo, X.-Y., Yan, D., Dang, X., Guo, L., Jia, T., & Wang, Q. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c00310 · Cited by 25

Nature-inspired and medicinally relevant short peptides

Ciulla, M. G., Civera, M., Sattin, S., & Kumar, K. (2023) · Exploration of Drug Science · doi:10.37349/eds.2023.00011 · Cited by 26

Capillary electrophoresis in the analysis of therapeutic peptides—A review

Štefánik, O., Majerová, P., Kováč, A., Mikuš, P., & Piešťanský, J. (2023) · Electrophoresis · doi:10.1002/elps.202300141 · Cited by 25

Therapeutic implications of novel peptides targeting ER–mitochondria Ca2+-flux systems

Kerkhofs, M., Bultynck, G., Vervliet, T., & Monaco, G. (2019) · Drug Discovery Today · doi:10.1016/j.drudis.2019.03.020 · Cited by 25

Peptide/Receptor Co-evolution Explains the Lipolytic Function of the Neuropeptide TLQP-21

Sahu, B. S., Rodriguez, P., Nguyen, M. E., Han, R., Cero, C., Razzoli, M., Piaggi, P., Laskowski, L. J., Pavličev, M., Muglia, L. J., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.101 · Cited by 24

MRGPRX2 activation as a rapid, high-throughput mechanistic-based approach for detecting peptide-mediated human mast cell degranulation liabilities

Lafleur, M. A., Werner, J. A., Fort, M. M., Lobenhofer, E. K., Balázs, M., & Goyos, A. (2020) · Journal of Immunotoxicology · doi:10.1080/1547691x.2020.1757793 · Cited by 24

Discovery of a Beetroot Protease Inhibitor to Identify and Classify Plant-Derived Cystine Knot Peptides

Retzl, B., Hellinger, R., Muratspahić, E., Pinto, M. E. F., Bolzani, V. S., & Gruber, C. W. (2020) · Journal of Natural Products · doi:10.1021/acs.jnatprod.0c00648 · Cited by 24

HelixDiff, a Score-Based Diffusion Model for Generating All-Atom α‑Helical Structures

Xie, X., Valiente, P. A., Kim, J., & Kim, P. M. (2024) · ACS Central Science · doi:10.1021/acscentsci.3c01488 · Cited by 21

Development of peptide therapeutics: A nonclinical safety assessment perspective

Mitra, M. S., DeMarco, S. J., Holub, B., Thiruneelakantapillai, L., & Thackaberry, E. A. (2020) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2020.104766 · Cited by 23

Hormone-like conopeptides – new tools for pharmaceutical design

Turner, A., Kaas, Q., & Craik, D. J. (2020) · RSC Medicinal Chemistry · doi:10.1039/d0md00173b · Cited by 24

Conjugation with gold nanoparticles improves the stability of the KT2 peptide and maintains its anticancer properties

Maraming, P., Daduang, J., & Kah, J. C. Y. (2021) · RSC Advances · doi:10.1039/d1ra05980g · Cited by 24

Customized blood-brain barrier shuttle peptide to increase AAV9 vector crossing the BBB and augment transduction in the brain

Zhang, X., Chai, Z., Lee Dobbins, A., Itano, M. S., Askew, C., Miao, Z., Niu, H., Samulski, R. J., & Li, C. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2021.121340 · Cited by 23

Protein and peptide engineering for chemical exchange saturation transfer imaging in the age of synthetic biology

Gilad, A. A., Bar‐Shir, A., Bricco, A. R., Mohanta, Z., & McMahon, M. T. (2022) · NMR in Biomedicine · doi:10.1002/nbm.4712 · Cited by 23

Hydroxyl Group-Targeted Conjugate and Its Self-Assembled Nanoparticle of Peptide Drug: Effect of Degree of Saturation of Fatty Acids and Modification of Physicochemical Properties

Park, J., Ngo, H. V., Jin, H., Lee, K. W., & Lee, B. (2022) · International Journal of Nanomedicine · doi:10.2147/ijn.s356804 · Cited by 23

Mass Spectrometry Approaches Empowering Neuropeptide Discovery and Therapeutics

Anapindi, K. D. B., Romanova, E. V., Checco, J. W., & Sweedler, J. V. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000423 · Cited by 24

The industrial design, translation, and development strategies for long-acting peptide delivery

Yang, B., dos Santos, A. G., Puri, S., Bak, A., & Zhou, L. (2022) · Expert Opinion on Drug Delivery · doi:10.1080/17425247.2022.2098276 · Cited by 26

Identification of antiviral peptide inhibitors for receptor binding domain of SARS-CoV-2 omicron and its sub-variants: an in-silico approach

Singh, S., Banavath, H. N., Godara, P., Naik, B., Srivastava, V., & Prusty, D. (2022) · 3 Biotech · doi:10.1007/s13205-022-03258-4 · Cited by 23

Accurate Prediction for Protein–Peptide Binding Based on High-Temperature Molecular Dynamics Simulations

Chen, J., Jiang, F., & Wu, Y. (2022) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.2c00743 · Cited by 24

The Research Progress of Bioactive Peptides Derived from Traditional Natural Products in China

Zhang, Y., Liu, L., Zhang, M., Li, S., Wu, J., Sun, Q., Ma, S., & Cai, W. (2023) · Molecules · doi:10.3390/molecules28176421 · Cited by 24

ACP-BC: A Model for Accurate Identification of Anticancer Peptides Based on Fusion Features of Bidirectional Long Short-Term Memory and Chemically Derived Information

Sun, M., Hu, H., Pang, W., & Zhou, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015447 · Cited by 23

Peptides from allergenic lipocalins bind to formyl peptide receptor 3 in human dendritic cells to mediate TH2 immunity

Klaver, D., Posch, B., Geisler, A., Hermann, M., Reider, N., & Heufler, C. (2019) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2019.07.008 · Cited by 23

A clean-up strategy for identification of circulating endogenous short peptides in human plasma by zwitterionic hydrophilic liquid chromatography and untargeted peptidomics identification

Piovesana, S., Cerrato, A., Antonelli, M., Benedetti, B., Capriotti, A. L., Cavaliere, C., Montone, C. M., & Laganà, A. (2019) · Journal of Chromatography A · doi:10.1016/j.chroma.2019.460699 · Cited by 23

Stimuli-Responsive Conformational Transformation of Peptides for Tunable Cytotoxicity

Lee, J., Oh, E., Lee, H., Kim, J.-W., Kim, H. G., Park, H. J., & Kim, C. (2019) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.9b00730 · Cited by 23

A simple and rapid LC-MS/MS and CE-MS/MS analytical strategy for the determination of therapeutic peptides in modern immunotherapeutics and biopharmaceutics

Piešťanský, J., Baráth, P., Majerová, P., Galba, J., Mikuš, P., Kováčech, B., & Kováč, A. (2020) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2020.113449 · Cited by 23

Protein–Peptide Binding Energetics under Crowded Conditions

Stadmiller, S. S., Aguilar, J. S., Parnham, S. R., & Pielak, G. J. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c05578 · Cited by 23

Small Molecule NF-κB Inhibitors as Immune Potentiators for Enhancement of Vaccine Adjuvants

Moser, B., Escalante-Buendia, Y., Steinhardt, R. C., Rosenberger, M. G., Cassaidy, B., Naorem, N., Chon, A. C., Nguyen, M. C., Tran, N., & Esser-Kahn, A. P. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.511513 · Cited by 23

Post-Assembly Modification of Peptides by Ligand-Enabled β-C(sp3)–H Arylation of Alanine at the C-Terminus: Overcoming the Inhibition Effect of Peptide Bonds

Li, M., Akintelu, S. A., & Yao, B. (2021) · Organic Letters · doi:10.1021/acs.orglett.1c01481 · Cited by 23

The Potential of Peptide-Based Inhibitors in Disrupting Protein–Protein Interactions for Targeted Cancer Therapy

Afonso, A. L., Cavaleiro, C. T., Castanho, M. A. R. B., Neves, V., & Cavaco, M. C. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073117 · Cited by 26

Acetylcholinesterase inhibitory activity of a naturally occurring peptide isolated from Boana pulchella (Anura: Hylidae) and its analogs

Sanchís, I., Spinelli, R., Aschemacher, N. A., Húmpola, M. V., & Siano, Á. (2020) · Amino Acids · doi:10.1007/s00726-019-02815-1 · Cited by 22

Strategies to expand peptide functionality through hybridisation with a small molecule component

Wu, Y., Williams, J. P. C., Calder, E. D. D., & Walport, L. J. (2020) · RSC Chemical Biology · doi:10.1039/d0cb00167h · Cited by 23

Systematic Development of Peptide Inhibitors Targeting the CXCL12/HMGB1 Interaction

Sgrignani, J., Cecchinato, V., Fassi, E. M. A., D’Agostino, G., Garofalo, M., Danelon, G., Pedotti, M., Simonelli, L., Varani, L., Grazioso, G., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00852 · Cited by 22

Peptide conjugates of 18β-glycyrrhetinic acid as potent inhibitors of α-glucosidase and AGEs-induced oxidation

Khan, S. N., Shaheen, F., Aleem, U., Sheikh, S., Tamfu, A. N., Ashraf, S., Ul‐Haq, Z., Ullah, S., Wahab, A., Choudhary, M. I., et al. (2021) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2021.106045 · Cited by 22

Mitochondrially-Targeted Therapeutic Strategies for Alzheimer’s Disease

Onyango, I. G., Bennett, J. P., & Stokin, G. B. (2021) · Current Alzheimer Research · doi:10.2174/1567205018666211208125855 · Cited by 22

Inhibition of the Interaction of TREM-1 and eCIRP Attenuates Inflammation and Improves Survival in Hepatic Ischemia/Reperfusion

Borjas, T., Jacob, A., Yen, H.-T., Patel, V. M., Coppa, G. F., Aziz, M., & Wang, P. (2021) · Shock · doi:10.1097/shk.0000000000001894 · Cited by 23

Umpolung Ala B Reagents for the Synthesis of Non‐Proteogenic Amino Acids, Peptides and Proteins**

Zhu, F., Miller, E., Powell, W. C., Johnson, K. C., Beggs, A., Evenson, G. E., & Walczak, M. A. A. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202207153 · Cited by 23

Peptide‐based diagnostic and therapeutic agents: Where we are and where we are heading?

Khalily, M. P., & Soydan, M. (2022) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14180 · Cited by 22

Bibliometric Review of the Literature on Cone Snail Peptide Toxins from 2000 to 2022

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