Rational design of stapled antimicrobial peptides

• Published in: Amino acids Vol. 55; no. 4; pp. 421 - 442
• Main Authors: You, YuHao, Liu, HongYu, Zhu, YouZhuo, Zheng, Heng
• Format: Journal Article
• Language: English
• Published: Vienna Springer Vienna 01.04.2023; Springer Nature B.V
• Subjects: Amino acid substitution; Amino acids; Analytical Chemistry; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - pharmacology; antibiotic resistance; Antibiotics; Antiinfectives and antibacterials; Antimicrobial agents; Antimicrobial Peptides; Artificial Intelligence; bioactive properties; Biochemical Engineering; Biochemistry; Biological activity; Biomedical and Life Sciences; Bridges; CAD; Chains; clinical trials; Computer aided design; Dipole moments; drug design; Drug development; Drug resistance; Helicity; Hydrophobicity; Innate immunity; Life Sciences; Microbial Sensitivity Tests; NCT NCT; NCT NCT0159476202576847; Neurobiology; Penetration resistance; Peptides; Physicochemical properties; Prospective Studies; Protein structure; proteinases; Proteomics; Review Article; Secondary structure; Stability; Structure-Activity Relationship; Stapled antimicrobial peptide; Antimicrobial activity; Hemolytic activity; Alpha helix; Computer design; Antimicrobial peptide

The global increase in antimicrobial drug resistance has dramatically reduced the effectiveness of traditional antibiotics. Structurally diverse antibiotics are urgently needed to combat multiple-resistant bacterial infections. As part of innate immunity, antimicrobial peptides have been recognized...