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The molecular design of a recombinant antimicrobial peptide CP and its in vitro activity.

Abstract：

:Antibacterial peptides from various sources express different antibacterial activity. In order to obtain a high activity antibacterial peptide, the sequences of four antimicrobial peptides--Protegrin-1, 4 kDa Scorpion Defensin, Metalnikowin-2A and Sheep Myeloid Antibacterial Peptide SMAP-29--were exploited to generate a synthetic antimicrobial peptide cp gene, which was then cloned into the expression vector pPICZalpha-A. The constructed recombinant expression vector pPICZalpha-cp was transformed into Pichia pastoris X-33, in which the synthetic antimicrobial peptide (CP) could be expressed under the control of the inducible AOX1 promoter and secreted via the alpha mating factor leader of Saccharomyces cerevisiae. Results showed that recombinant plasmid is highly stable, and In vitro experiments showed that the recombinant antimicrobial peptide CP is heat and acid-stable, and it has high antibacterial activity against several Gram-positive and -negative bacteria. Only 1 microg of the recombinant antimicrobial peptide CP has an antibacterial activity equivalent to 64 U ampicillin. Thus, this recombinant antimicrobial peptide could serve as an attractive candidate for the development of therapeutic antimicrobial drugs.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Niu M,Li X,Wei J,Cao R,Zhou B,Chen P

doi

10.1016/j.pep.2007.08.006

subject

Has Abstract

pub_date

2008-01-01 00:00:00

pages

95-100

issue

1

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(07)00196-9

journal_volume

57

pub_type

杂志文章

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