Dihydrofolate reductase inhibitory peptides screened from a structured designed β-loop peptide library displayed on phage

Enzyme inhibitory peptides with a loop structure stabilized using an antiparallel β-sheet scaffold (β-loop peptide) were obtained from a designed peptide phage library.

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A Novel Peptide Isolated from a Phage Display Peptide Library Modeling Antigenic Epitope of DHAV-1 and DHAV-3

Vaccines ◽

10.3390/vaccines8010121 ◽

2020 ◽

Vol 8 (1) ◽

pp. 121

Author(s):

Ruihua Zhang ◽

Yupeng Yang ◽

Jingjing Lan ◽

Shaoli Lin ◽

Zhijing Xie ◽

...

Keyword(s):

Phage Display ◽

Hepatitis A Virus ◽

Protein A ◽

Neutralizing Antibody ◽

Peptide Library ◽

Phage Library ◽

Structural Protein ◽

Phage Display Technology ◽

Duck Hepatitis ◽

Phage Display Peptide Library

Duck hepatitis A virus (DHAV), the major pathogen of duck virus hepatitis (DVH), causes severe diseases that threaten the duck industry worldwide. The VP1 protein, a major structural protein of DHAV, is able to induce neutralizing antibody in ducks. The purpose of this study was to identify the antigenic mimotope of DHAV by phage display technology. A monoclonal antibody (mAb) 4E6 against DHAV-1 and DHAV-3 was prepared, and a phage library prepared with the PhD-12 Phage Display Peptide Library Kit was screened with the mAb. A novel peptide, 1GLTWKLPPSM10 was identified with high affinity to the mAb and could specifically block mAb 4E6 from binding DHAV-1 and DHAV-3. Animal tests confirmed that the immunization of ducklings with the mimotope could inhibit the virus proliferation and protect the ducklings from DVH. In summary, the neutralizing conformational mimotope 1GLTWKLPPSM10 might be a promising vaccine candidate for the prevention of DHAV infection.

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Generation of inhibitory peptides for IKKε from a kinase‐focused phage library of helix‐loop‐helix peptides

Peptide Science ◽

10.1002/pep2.24253 ◽

2021 ◽

Author(s):

Kousuke Mihara ◽

Natsumi Nakajima ◽

Ikuo Fujii ◽

Daisuke Fujiwara

Keyword(s):

Phage Library ◽

Inhibitory Peptides ◽

Helix Loop Helix

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Screening of ACE-inhibitory peptides from a random peptide-displayed phage library using ACE-coupled liposomes

Journal of Biotechnology ◽

10.1016/j.jbiotec.2007.06.003 ◽

2007 ◽

Vol 131 (2) ◽

pp. 144-149 ◽

Cited By ~ 8

Author(s):

Yoichi Kumada ◽

Naoya Hashimoto ◽

Fida Hasan ◽

Masaaki Terashima ◽

Kazuhiro Nakanishi ◽

...

Keyword(s):

Phage Library ◽

Random Peptide ◽

Inhibitory Peptides ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

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Structure-Function Relationship Studies on the Frog Skin Antimicrobial Peptide Tigerinin 1: Design of Analogs with Improved Activity and Their Action on Clinical Bacterial Isolates

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.46.7.2279-2283.2002 ◽

2002 ◽

Vol 46 (7) ◽

pp. 2279-2283 ◽

Cited By ~ 27

Author(s):

Narasimhaiah Sitaram ◽

Korrapati Purna Sai ◽

Shashi Singh ◽

Krishnan Sankaran ◽

Ramakrishnan Nagaraj

Keyword(s):

Antimicrobial Peptides ◽

Structure Function ◽

Disulfide Bridge ◽

Structural Basis ◽

Loop Structure ◽

Disulfide Bridges ◽

Bacterial Isolates ◽

Optimal Activity ◽

Function Relationship ◽

Β Sheet

ABSTRACT Structure-function relationships in antimicrobial peptides have been extensively investigated in order to obtain improved analogs. Most of these studies have targeted either α-helical peptides or β-sheet peptides with multiple disulfide bridges. Tigerinins are short, nonhelical antimicrobial peptides with a single disulfide bridge. In this study, we have synthesized several analogs of tigerinin 1 with an aim to understand the structural basis of activity as well as improve its activity. The studies demonstrate that the loop structure of tigerinin 1 is essential for its optimal activity. However, linearization with increased cationic charges can compensate for loss of loop structure to some extent. Morphology of the cells after treatment with the active analogs shows extensive leakage of cytoplasmic contents. Tigerinin 1 and two of its analogs exhibit impressive activity against a variety of clinical bacterial isolates.

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High-resolution gold labeling

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100147491 ◽

1993 ◽

Vol 51 ◽

pp. 330-331

Author(s):

James F. Hainfeld ◽

Frederic R. Furuya ◽

Kyra Carbone ◽

Martha Simon ◽

Beth Lin ◽

...

Keyword(s):

Dihydrofolate Reductase ◽

Polypeptide Chain ◽

External Surface ◽

Gold Cluster ◽

Macromolecular Complex ◽

Gold Compound ◽

Central Cavity ◽

Chain Folding ◽

E Coli ◽

Chaperonin Groel

A recently developed 1.4 nm gold cluster has been found to be useful in labeling macromolecular sites to 1-3 nm resolution. The gold compound is organically derivatized to contain a monofunctional arm for covalent linking to biomolecules. This may be used to mark a specific site on a structure, or to first label a component and then reassemble a multicomponent macromolecular complex. Two examples are given here: the chaperonin groEL and ribosomes.Chaperonins are essential oligomeric complexes that mediate nascent polypeptide chain folding to produce active proteins. The E. coli chaperonin, groEL, has two stacked rings with a central hole ∽6 nm in diameter. The protein dihydrofolate reductase (DHFR) is a small protein that has been used in chain folding experiments, and serves as a model substrate for groEL. By labeling the DHFR with gold, its position with respect to the groEL complex can be followed. In particular, it was sought to determine if DHFR refolds on the external surface of the groEL complex, or whether it interacts in the central cavity.

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