ATP selection in a random peptide library consisting of prebiotic amino acids

Shou Kai Kang; Bai Xue Chen; Tian Tian; Xi Shuai Jia; Xin Yi Chu; Rong Liu; Peng Fei Dong; Qing Yong Yang; Hong Yu Zhang

doi:10.1016/j.bbrc.2015.09.038

ATP selection in a random peptide library consisting of prebiotic amino acids

Shou Kai Kang, Bai Xue Chen, Tian Tian, Xi Shuai Jia, Xin Yi Chu, Rong Liu, Peng Fei Dong, Qing Yong Yang, Hong Yu Zhang

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

Based upon many theoretical findings on protein evolution, we proposed a ligand-selection model for the origin of proteins, in which the most ancient proteins originated from ATP selection in a pool of random peptides. To test this ligand-selection model, we constructed a random peptide library consisting of 15 types of prebiotic amino acids and then used cDNA display to perform six rounds of in vitro selection with ATP. By means of next-generation sequencing, the most prevalent sequence was defined. Biochemical and biophysical characterization of the selected peptide showed that it was stable and foldable and had ATP-hydrolysis activity as well.

Original language	English
Pages (from-to)	400-405
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	466
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2015.09.038
State	Published - 23 Oct 2015
Externally published	Yes

Keywords

In vitro selection
Next-generation sequencing
Origin of proteins
Protein evolution
Structure and function
cDNA display

Access to Document

10.1016/j.bbrc.2015.09.038

Cite this

@article{0cc2d8c90d2b4c9ca3c2fda7753a2430,

title = "ATP selection in a random peptide library consisting of prebiotic amino acids",

abstract = "Based upon many theoretical findings on protein evolution, we proposed a ligand-selection model for the origin of proteins, in which the most ancient proteins originated from ATP selection in a pool of random peptides. To test this ligand-selection model, we constructed a random peptide library consisting of 15 types of prebiotic amino acids and then used cDNA display to perform six rounds of in vitro selection with ATP. By means of next-generation sequencing, the most prevalent sequence was defined. Biochemical and biophysical characterization of the selected peptide showed that it was stable and foldable and had ATP-hydrolysis activity as well.",

keywords = "In vitro selection, Next-generation sequencing, Origin of proteins, Protein evolution, Structure and function, cDNA display",

author = "Kang, {Shou Kai} and Chen, {Bai Xue} and Tian Tian and Jia, {Xi Shuai} and Chu, {Xin Yi} and Rong Liu and Dong, {Peng Fei} and Yang, {Qing Yong} and Zhang, {Hong Yu}",

year = "2015",

month = oct,

day = "23",

doi = "10.1016/j.bbrc.2015.09.038",

language = "English",

volume = "466",

pages = "400--405",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "3",

}

TY - JOUR

T1 - ATP selection in a random peptide library consisting of prebiotic amino acids

AU - Kang, Shou Kai

AU - Chen, Bai Xue

AU - Tian, Tian

AU - Jia, Xi Shuai

AU - Chu, Xin Yi

AU - Liu, Rong

AU - Dong, Peng Fei

AU - Yang, Qing Yong

AU - Zhang, Hong Yu

PY - 2015/10/23

Y1 - 2015/10/23

N2 - Based upon many theoretical findings on protein evolution, we proposed a ligand-selection model for the origin of proteins, in which the most ancient proteins originated from ATP selection in a pool of random peptides. To test this ligand-selection model, we constructed a random peptide library consisting of 15 types of prebiotic amino acids and then used cDNA display to perform six rounds of in vitro selection with ATP. By means of next-generation sequencing, the most prevalent sequence was defined. Biochemical and biophysical characterization of the selected peptide showed that it was stable and foldable and had ATP-hydrolysis activity as well.

AB - Based upon many theoretical findings on protein evolution, we proposed a ligand-selection model for the origin of proteins, in which the most ancient proteins originated from ATP selection in a pool of random peptides. To test this ligand-selection model, we constructed a random peptide library consisting of 15 types of prebiotic amino acids and then used cDNA display to perform six rounds of in vitro selection with ATP. By means of next-generation sequencing, the most prevalent sequence was defined. Biochemical and biophysical characterization of the selected peptide showed that it was stable and foldable and had ATP-hydrolysis activity as well.

KW - In vitro selection

KW - Next-generation sequencing

KW - Origin of proteins

KW - Protein evolution

KW - Structure and function

KW - cDNA display

UR - http://www.scopus.com/inward/record.url?scp=84943358010&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2015.09.038

DO - 10.1016/j.bbrc.2015.09.038

M3 - Article

C2 - 26365351

AN - SCOPUS:84943358010

SN - 0006-291X

VL - 466

SP - 400

EP - 405

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

ATP selection in a random peptide library consisting of prebiotic amino acids

Abstract

Keywords

Access to Document

Fingerprint

Cite this