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You searched for: Author "Zuo, Xiaobing" Remove constraint Author: "Zuo, Xiaobing" Subject X-radiation Remove constraint Subject: X-radiation Subject amino acids Remove constraint Subject: amino acids
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1. Helical 1:1 α/Sulfono-γ-AA Heterogeneous Peptides with Antibacterial Activity

Author:
Zuo, Xiaobing,   et al.   ; She, Fengyu; Nimmagadda, Alekhya; Teng, Peng; Su, Ma; Cai, Jianfeng;     Show all 6 Authors
Source:
Biomacromolecules 2016 v.17 no.5 pp. 1854-1859
ISSN:
1526-4602
Subject:
Gram-negative bacteria; X-radiation; amino acids; antibacterial properties; antibiotic resistance; cell death; fluorescence microscopy; multiple drug resistance; pathogens; peptides; protein-protein interactions; public health
Abstract:
... As one of the greatest threats facing the 21st century, antibiotic resistance is now a major public health concern. Host-defense peptides (HDPs) offer an alternative approach to combat emerging multi-drug-resistant bacteria. It is known that helical HDPs such as magainin 2 and its analogs adopt cationic amphipathic conformations upon interaction with bacterial membranes, leading to membrane disrup ...
DOI:
10.1021/acs.biomac.6b00286
PubMed:
27030636
PubMed Central:
PMC5340309

2. New Class of Heterogeneous Helical Peptidomimetics

Author:
Zuo, Xiaobing,   et al.   ; Wu, Haifan; Qiao, Qiao; Teng, Peng; Hu, Yaogang; Antoniadis, Dimitrios; Cai, Jianfeng;     Show all 7 Authors
Source:
Organic letters 2015 v.17 no.14 pp. 3524-3527
ISSN:
1523-7052
Subject:
X-radiation; amino acids; chemical reactions; chemical structure; circular dichroism spectroscopy; nuclear magnetic resonance spectroscopy; organic compounds; peptides; temperature
Abstract:
... A new class of unnatural heterogeneous foldamers is reported to contain alternative α-amino acid and sulfono-γ-AA amino acid residues in a 1:1 repeat pattern. Two-dimensional NMR data show that two 1:1 α/sulfono-γ-AA peptides with diverse side chains form analogous right-handed helical structures in solution. The effects of sequence length, side chain, N-capping, and temperature on folding propens ...
DOI:
10.1021/acs.orglett.5b01608