Amino group binding peptide aptamers with double disulphide-bridged loops selected by in vitro selection using cDNA display

2014 ◽  
Vol 50 (42) ◽  
pp. 5608-5610 ◽  
Author(s):  
Yuki Mochizuki ◽  
Koichi Nishigaki ◽  
Naoto Nemoto
Keyword(s):  
In Vitro Selection ◽  
Amino Group ◽  
Peptide Aptamers ◽  
Binding Peptide ◽  
Peptide Aptamer

Double disulphide-bridged loops of peptide aptamer are indispensable for the amino group recognition.

In vitro selection of a photoresponsive peptide aptamer to glutathione-immobilized microbeads

2015 ◽  
Vol 119 (2) ◽  
pp. 137-139 ◽  
Author(s):  
Seiichi Tada ◽  
Qingmin Zang ◽  
Wei Wang ◽  
Masuki Kawamoto ◽  
Mingzhe Liu ◽  
...  
Keyword(s):  
In Vitro Selection ◽  
Peptide Aptamer ◽  
Selection Of

scholarly journals In Vitro Selection of Cathepsin E-Activity-Enhancing Peptide Aptamers at Neutral pH

2011 ◽  
Vol 2011 ◽  
pp. 1-10 ◽  
Author(s):  
Madhu Biyani ◽  
Masae Futakami ◽  
Koichiro Kitamura ◽  
Tomoyo Kawakubo ◽  
Miho Suzuki ◽  
...  
Keyword(s):  
In Vitro Selection ◽  
Physiological Activity ◽  
Peptide Aptamers ◽  
Neutral Ph ◽  
Cathepsin E ◽  
Analysis System ◽  
Ph Range ◽  
Cancerous Cells ◽  
Inverse Substrate

The aspartic protease cathepsin E has been shown to induce apoptosis in cancer cells under physiological conditions. Therefore, cathepsin E-activity-enhancing peptides functioning in the physiological pH range are valuable potential cancer therapeutic candidates. Here, we have used a general in vitro selection method (evolutionary rapid panning analysis system (eRAPANSY)), based on inverse substrate-function link (SF-link) selection to successfully identify cathepsin E-activity-enhancing peptide aptamers at neutral pH. A successive enrichment of peptide activators was attained in the course of selection. One such peptide activated cathepsin E up to 260%, had a high affinity (KD; ∼300 nM), and had physiological activity as demonstrated by its apoptosis-inducing reaction in cancerous cells. This method is expected to be widely applicable for the identification of protease-activity-enhancing peptide aptamers.

scholarly journals DNAzymes for Amine and Peptide Lysine Acylation

2020 ◽  
Author(s):  
Tianjiong Yao ◽  
Jack Przybyla ◽  
Peter Yeh ◽  
Austin Woodard ◽  
Hannah Nilsson ◽  
...  
Keyword(s):  
Chemical Reactions ◽  
In Vitro Selection ◽  
Side Chains ◽  
Amino Group ◽  
Biologically Relevant ◽  
Protein Substrates ◽  
Peptide Modifications ◽  
Selection For ◽  
Acyl Donors

DNAzymes were previously identified by in vitro selection for a variety of chemical reactions, including several biologically relevant peptide modifications. However, finding DNAzymes for peptide lysine acylation is a substantial challenge. By using suitably reactive aryl ester acyl donors as the electrophiles, here we used in vitro selection to identify DNAzymes that acylate amines, including lysine side chains of DNA-anchored peptides. Some of the DNAzymes can transfer a small glutaryl group to an amino group. These results expand the scope of DNAzyme catalysis and suggest the future broader applicability of DNAzymes for sequence-selective lysine acylation of peptide and protein substrates.

In vitro selection of peptide aptamers using a ribosome display for a conducting polymer

2014 ◽  
Vol 117 (4) ◽  
pp. 501-503 ◽  
Author(s):  
Zha Li ◽  
Takanori Uzawa ◽  
Haichao Zhao ◽  
Shyh-Chyang Luo ◽  
Hsiao-hua Yu ◽  
...  
Keyword(s):  
Conducting Polymer ◽  
In Vitro Selection ◽  
Ribosome Display ◽  
Peptide Aptamers ◽  
Selection Of

In vitro selection of a photo-responsive peptide aptamer using ribosome display

2012 ◽  
Vol 48 (97) ◽  
pp. 11871 ◽  
Author(s):  
Mingzhe Liu ◽  
Seiichi Tada ◽  
Mika Ito ◽  
Hiroshi Abe ◽  
Yoshihiro Ito
Keyword(s):  
In Vitro Selection ◽  
Ribosome Display ◽  
Peptide Aptamer ◽  
Selection Of

scholarly journals 2P312 In vitro selection of peptide aptamer binding to reduced ferredoxin(28. Bioengineering,Poster)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S210
Author(s):  
Yasodha Manandhar ◽  
Takanori Uzawa ◽  
Toshiro Aigaki ◽  
Yoshihiro Ito
Keyword(s):  
In Vitro Selection ◽  
Peptide Aptamer ◽  
Selection Of

In vitro selection of a peptide aptamer that changes fluorescence in response to verotoxin

2014 ◽  
Vol 37 (3) ◽  
pp. 619-625 ◽  
Author(s):  
Yasodha Manandhar ◽  
K. C. Tara Bahadur ◽  
Wei Wang ◽  
Takanori Uzawa ◽  
Toshiro Aigaki ◽  
...  
Keyword(s):  
In Vitro Selection ◽  
Peptide Aptamer ◽  
Selection Of

In vitro selection of peptide aptamers with affinity to single-wall carbon nanotubes using a ribosome display

2012 ◽  
Vol 35 (1) ◽  
pp. 39-45 ◽  
Author(s):  
Zha Li ◽  
Takanori Uzawa ◽  
Takashi Tanaka ◽  
Akira Hida ◽  
Koji Ishibashi ◽  
...  
Keyword(s):  
Carbon Nanotubes ◽  
In Vitro Selection ◽  
Single Wall Carbon Nanotubes ◽  
Ribosome Display ◽  
Peptide Aptamers ◽  
Single Wall Carbon ◽  
Selection Of

scholarly journals An RNA Binding Peptide Consisting of Four Types of Amino Acid by in Vitro Selection Using cDNA Display

ACS Omega ◽  
2016 ◽  
Vol 1 (1) ◽  
pp. 52-57 ◽  
Author(s):  
Shigefumi Kumachi ◽  
Yuzuru Husimi ◽  
Naoto Nemoto
Keyword(s):  
Amino Acid ◽  
In Vitro Selection ◽  
Rna Binding ◽  
Binding Peptide

scholarly journals DNAzymes for Amine and Peptide Lysine Acylation

2020 ◽  
Author(s):  
Tianjiong Yao ◽  
Jack Przybyla ◽  
Peter Yeh ◽  
Austin Woodard ◽  
Hannah Nilsson ◽  
...  
Keyword(s):  
Chemical Reactions ◽  
In Vitro Selection ◽  
Side Chains ◽  
Amino Group ◽  
Biologically Relevant ◽  
Protein Substrates ◽  
Peptide Modifications ◽  
Selection For ◽  
Acyl Donors

DNAzymes were previously identified by in vitro selection for a variety of chemical reactions, including several biologically relevant peptide modifications. However, finding DNAzymes for peptide lysine acylation is a substantial challenge. By using suitably reactive aryl ester acyl donors as the electrophiles, here we used in vitro selection to identify DNAzymes that acylate amines, including lysine side chains of DNA-anchored peptides. Some of the DNAzymes can transfer a small glutaryl group to an amino group. These results expand the scope of DNAzyme catalysis and suggest the future broader applicability of DNAzymes for sequence-selective lysine acylation of peptide and protein substrates.

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