A conformation-constrained peptide library based on insect defensin A
| Autor: | Jiannan Feng, Nongle Liu, Huixin Wang, Can-quan Mao, Fang Wang, Yanning Xue, Bo Gao, An Zhao, Zheng Li, Jie Zhang |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Scaffold protein
alpha-Defensins Insecta Physiology Recombinant Fusion Proteins Molecular Sequence Data Peptide Biology Biochemistry Cellular and Molecular Neuroscience Endocrinology Protein structure Peptide Library Animals Receptors Tumor Necrosis Factor Type II Amino Acid Sequence Peptide library Peptide sequence Defensin chemistry.chemical_classification Tumor Necrosis Factor-alpha Antibodies Monoclonal biology.organism_classification Molecular biology Protein Structure Tertiary Amino acid Amino Acid Substitution chemistry Filamentous bacteriophage Receptors Tumor Necrosis Factor Type I Capsid Proteins Software Bacteriophage M13 Protein Binding |
| Zdroj: | Peptides. 25:629-635 |
| ISSN: | 0196-9781 |
| DOI: | 10.1016/j.peptides.2004.01.022 |
| Popis: | Here, we reported a conformation-constrained peptide library, that was constructed based on the scaffold of a 29 amino acids peptide derived from insect defensin A. The peptide scaffold was designed utilizing the InsightII molecular modeling software and then displayed on M13 filamentous bacteriophage by fusion with coat protein III. The library was constructed by randomization of seven positions located within the two loops of the peptide scaffold generating approximately 8.3 x 10(8) transformants. Sequences from 14 randomly selected phage clones indicated that the distribution of nucleotides and amino acids paralleled with the expected frequency. Screening against the target proteins: tumor necrosis factor alpha, TNF receptor 1, TNF receptor 2 and monoclonal antibody against BMP-2 showed significant enrichment in all cases. The results presented here show that the reconstructed insect defensin A domain will be a promising non-antibody protein scaffold for the presentation of a phage-displayed constrained peptide library. |
| Databáze: | OpenAIRE |
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