Structure, function and molecular design strategies of antibacterial peptide SMAP-29: a review / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 846-859, 2011.
Article
in Chinese
| WPRIM
| ID: wpr-324494
ABSTRACT
Antibacterial peptides are a family of host-defense peptides most of which are gene-encoded and produced by living organisms of all types. Antibacterial peptides are small molecular proteins with broad antimicrobial spectrum against bacteria, viruses, fungi and sometimes even as anticancer peptide. SMAP-29, a cathelicidin-like peptide derived from sheep myeloid, line alpha-helical Structure, exerts a powerful broad antimicrobial activity against different pathogens including Gram-positive and Gram-negative bacteria, fungi, viruses, parasites, spirochaetes, chlamydia and antiendotoxin activity, and particular antibacterial mechanism, rapidly to permeabilize membranes of susceptible organisms. This paper summarizes the lately research progress of SMAP-29 and Variants including the characteristics of structure, structure-activity relationships, mode of action, diverse biological functions, gene recombinant and expression. We put emphasis on the necessity of molecular design, and primary and secondary structure-based modification, to provides a strong foundation for further drug development and design of SMAP-29.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Physiology
/
Recombinant Proteins
/
Sheep
/
Blood Proteins
/
Drug Design
/
Chemistry
/
Antimicrobial Cationic Peptides
/
Cathelicidins
/
Genetics
Type of study:
Prognostic study
Limits:
Animals
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2011
Type:
Article
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