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Investigation of α/γ hybrid peptide self‐assembled structures with antimicrobial and antibiofilm properties
Author(s) -
Shankar Sudha,
Singh Gurpreet,
Rahim Junaid Ur,
Qayum Arem,
Sharma Parduman R.,
Katoch Meenu,
Rai Rajkishor
Publication year - 2020
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3243
Subject(s) - circular dichroism , peptide , chemistry , biofilm , klebsiella pneumoniae , antibacterial activity , escherichia coli , self assembly , dimethyl sulfoxide , antimicrobial , sulfoxide , combinatorial chemistry , pseudomonas aeruginosa , stereochemistry , biochemistry , organic chemistry , bacteria , biology , gene , genetics
The present work describes the synthesis and characterization of α/γ hybrid peptides, Boc‐Phe‐γ 4 ‐Phe‐Val‐OMe, P1 ; Boc‐Ala‐γ 4 ‐Phe‐Val‐OMe, P2 ; and Boc‐Leu‐γ 4 ‐Phe‐Val‐OMe, P3 together with the formation of self‐assembled structures formed by these hybrid peptides in dimethyl sulfoxide (DMSO)/water (1:1). The self‐assembled structures were characterized by infrared (IR) spectroscopy, circular dichroism (CD), and scanning electron microscopy (SEM). Further, α/γ hybrid peptide self‐assembled structures were evaluated for antibacterial properties. Among all, the self‐assembled peptide P1 exhibited the antimicrobial activity against Escherichia coli and Klebsiella pneumoniae , while self‐assembled peptide P3 inhibited the biofilms of Salmonella typhimurium and Pseudomonas aeruginosa . In this study, we have shown the significance of self‐assembled structures formed from completely hydrophobic α/γ hybrid peptides in exploring the antibacterial properties together with biofilm inhibition.