Literature DB >> 12590458

Homology similarity analysis of sequences of lactoferricin and its derivatives.

Shuryo Nakai1, Judy C K Chan, Eunice C Y Li-Chan, Jinglie Dou, Masahiro Ogawa.   

Abstract

A new method, homology similarity analysis (HSA), was developed to investigate homology pattern similarities of selected segments within sequences of peptides. This new approach facilitated elucidation of the structure-function relationships of lactoferricin derivatives. Helix propensity of positions 4-9 in the lactoferricin sequence was the most important in determining the antimicrobial activity of lactoferricin against Escherichia coli, followed by cationic charge pattern at positions 4-9 and 1-3. The pattern similarity of segments within sequences could be a useful tool for representing the distribution attributes of amino acid residue properties to the structure-function relationships of proteins and peptides, especially when used in conjunction with principal component similarity analysis followed by the regression version of artificial neural networks.

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Year:  2003        PMID: 12590458     DOI: 10.1021/jf0206062

Source DB:  PubMed          Journal:  J Agric Food Chem        ISSN: 0021-8561            Impact factor:   5.279


  2 in total

1.  Pattern similarity study of functional sites in protein sequences: lysozymes and cystatins.

Authors:  Shuryo Nakai; Eunice C Y Li-Chan; Jinglie Dou
Journal:  BMC Biochem       Date:  2005-05-18       Impact factor: 4.059

2.  Penetration of milk-derived antimicrobial peptides into phospholipid monolayers as model biomembranes.

Authors:  Wanda Barzyk; Ewa Rogalska; Katarzyna Więcław-Czapla
Journal:  Biochem Res Int       Date:  2013-12-17
  2 in total

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