Deletion of All Cysteines in Tachyplesin I Abolishes Hemolytic Activity and Retains Antimicrobial Activity and LPS Selective Binding†

Autor: Ramamoorthy, Ayyalusamy, Thennarasu, Sathiah, Tan, Anmin, Gottipati, Kiran, Sreekumar, Sreeja, Heyl, Deborah L., An, Florence Y.P., Shelburne, Charles E.

Tachyplesin I is a cyclic beta-sheet antimicrobial peptide isolated from the hemocytes of Tachypleus tridentatus. The four cysteine residues in tachyplesin I play a structural role in imparting amphipathicity to the peptide which has been shown to be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::43a768592f021a2778d050180c3b0651
https://europepmc.org/articles/PMC2515376/

Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective binding.

Autor: Ramamoorthy A; Department of Chemistry and Biophysics Research Division, The University of Michigan, Ann Arbor, Michigan 48109-1055, USA. ramamoor@umich.edu, Thennarasu S, Tan A, Gottipati K, Sreekumar S, Heyl DL, An FY, Shelburne CE

Publikováno v: Biochemistry [Biochemistry] 2006 May 23; Vol. 45 (20), pp. 6529-40.