Influences of disulfide connectivity on structure and antimicrobial activity of tachyplesin I

Author:

Shi Juan12,So Lok-Yan3,Chen Fangling12,Liang Jiazhen12,Chow Ho-Yin3,Wong Kwok-Yin3,Wan Shengbiao12,Jiang Tao12,Yu Rilei12ORCID

Affiliation:

1. Key Laboratory of Marine Drugs, Chinese Ministry of Education, School of Medicine and Pharmacy; Ocean University of China; Qingdao 266003 China

2. Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology; Qingdao 266003 China

3. Department of Applied Biology and Chemical Technology and the State Key Laboratory of Chirosciences; The Hong Kong Polytechnic University; Hong Kong

Funder

National Natural Science Foundation of China

Central Universities

Qingdao National Laboratory for Marine Science and Technology

Publisher

Wiley

Subject

Organic Chemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,General Medicine,Biochemistry,Structural Biology

Reference30 articles.

1. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure;Nakamura;J Biol Chem,1988

2. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: Chemical structures and biological activity;Miyata;J Biochem,1989

3. Marked increase in membranolytic selectivity of novel cyclic tachyplesins constrained with an antiparallel two-beta strand cystine knot framework;Tam;Biochem Biophys Res Commun,2000

4. Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the horseshoe crab (Tachypleus tridentatus). NMR determination of the beta-sheet structure;Kawano;J Biol Chem,1990

5. Structural effects of tachyplesin I and its linear derivative on their aggregation and mobility in lipid bilayers;Han;J Mol Graph Model,2015

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