Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity | Zendy

Emiliano Salvucci | Zendy; Lucila Saavedra | Zendy; Fernando Sesma | Zendy

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Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity

Author(s) -

Emiliano Salvucci,

Lucila Saavedra,

Fernando Sesma

Publication year - 2007

Publication title -

journal of antimicrobial chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.124

H-Index - 194

eISSN - 1460-2091

pISSN - 0305-7453

DOI - 10.1093/jac/dkm096

Subject(s) - bacteriocin , peptide , antimicrobial peptides , antimicrobial , listeria monocytogenes , listeria , subclass , biochemistry , chemistry , peptide sequence , bacteria , biology , microbiology and biotechnology , genetics , gene , antibody , immunology

Subclass IIa bacteriocins are characterized by a hydrophilic N-terminal domain that shares a YGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Enterocin CRL35 is a 43-amino-acid heat stable peptide with antilisterial activity. Short synthetic peptides derived from the N-terminal half of enterocin CRL35 and other subclass IIa bacteriocins were evaluated for antimicrobial properties.

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