Identification of a Novel Skin Penetration Enhancement Peptide by Phage Display Peptide Library Screening

2012 ◽  
Vol 9 (5) ◽  
pp. 1320-1330 ◽  
Author(s):  
Sunny Kumar ◽  
Preety Sahdev ◽  
Omathanu Perumal ◽  
Hemachand Tummala
Keyword(s):  
Phage Display ◽  
Skin Penetration ◽  
Peptide Library ◽  
Library Screening ◽  
Penetration Enhancement ◽  
Phage Display Peptide Library

Identification of rabies virus mimotopes screened from a phage display peptide library with purified dog anti-rabies virus serum IgG

2013 ◽  
Vol 174 (1-2) ◽  
pp. 47-51 ◽  
Author(s):  
Limin Yang ◽  
Junyu Cen ◽  
Qinghua Xue ◽  
Jing Li ◽  
Yuhai Bi ◽  
...  
Keyword(s):  
Phage Display ◽  
Rabies Virus ◽  
Peptide Library ◽  
Phage Display Peptide Library ◽  
Serum Igg

Identification of PSA peptide mimotopes using phage display peptide library

Peptides ◽  
2011 ◽  
Vol 32 (6) ◽  
pp. 1097-1102 ◽  
Author(s):  
Arulkumaran Shanmugam ◽  
Robert Suriano ◽  
Devyani Chaudhuri ◽  
Shilpi Rajoria ◽  
Andrea George ◽  
...  
Keyword(s):  
Phage Display ◽  
Peptide Library ◽  
Phage Display Peptide Library ◽  
Peptide Mimotopes

A synthetic peptide with estrogen-like activity derived from a phage-display peptide library

Peptides ◽  
2002 ◽  
Vol 23 (3) ◽  
pp. 573-580 ◽  
Author(s):  
Natarajan Venkatesh ◽  
Yehudith Zaltsman ◽  
Dalia Somjen ◽  
Batya Gayer ◽  
Ettickan Boopathi ◽  
...  
Keyword(s):  
Phage Display ◽  
Synthetic Peptide ◽  
Peptide Library ◽  
Phage Display Peptide Library

Identification of antigenic epitopes of the SapA protein of Campylobacter fetus using a phage display peptide library

2012 ◽  
Vol 93 (3) ◽  
pp. 1274-1280
Author(s):  
Hailing Zhao ◽  
Shenye Yu ◽  
Huifang Liu ◽  
Wei Si ◽  
Chunlai Wang ◽  
...  
Keyword(s):  
Phage Display ◽  
Peptide Library ◽  
Phage Display Peptide Library ◽  
Campylobacter Fetus ◽  
Antigenic Epitopes

scholarly journals The mimic epitopes ofMycobacterium tuberculosisscreened by phage display peptide library have serodiagnostic potential for tuberculosis

2016 ◽  
Vol 74 (8) ◽  
pp. ftw091 ◽  
Author(s):  
Li Wang ◽  
Xiangying Deng ◽  
Haican Liu ◽  
Lanhua Zhao ◽  
Xiaolong You ◽  
...  
Keyword(s):  
Phage Display ◽  
Peptide Library ◽  
Phage Display Peptide Library

scholarly journals Novel Method for Selection of Antimicrobial Peptides from a Phage Display Library by Use of Bacterial Magnetic Particles

2008 ◽  
Vol 74 (24) ◽  
pp. 7600-7606 ◽  
Author(s):  
Tsuyoshi Tanaka ◽  
Yoriko Kokuryu ◽  
Tadashi Matsunaga
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Phage Display ◽  
Magnetic Particles ◽  
Peptide Library ◽  
Inner Membrane ◽  
Phage Display Peptide Library ◽  
Wide Range ◽  
Bacterial Magnetic Particles ◽  
Selection Of

ABSTRACT Antimicrobial peptides were isolated from a phage display peptide library using bacterial magnetic particles (BacMPs) as a solid support. The BacMPs obtained from “Magnetospirillum magneticum” strain AMB-1 consist of pure magnetite (50 to 100 nm in size) and are covered with a lipid bilayer membrane derived from the invagination of the inner membrane. BacMPs are easily purified from a culture of magnetotactic bacteria by magnetic separation. Approximately 4 × 1010 PFU of the library phage (complexity, 2.7 × 109) was reacted with BacMPs. The elution of bound phages from BacMPs was performed by disrupting its membrane with phospholipase D treatment. Six candidate peptides, which were highly cationic and could bind onto the BacMP membrane, were obtained. They exhibited antimicrobial activity against Bacillus subtilis but not against Escherichia coli and Saccharomyces cerevisiae. The amino acid substitution of the selected peptide, KPQQHNRPLRHK (peptide 6-7), to enhance the hydrophobicity resulted in obvious antimicrobial activity against all test microorganisms. The present study shows for the first time that a magnetic selection of antimicrobial peptides from the phage display peptide library was successfully achieved by targeting the actual bacterial inner membrane. This BacMP-based method could be a promising approach for a high-throughput screening of antimicrobial peptides targeting a wide range of species.

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