Abstract:
OBJECTIVES:We examined the importance of aptamer usage under the same condition as the selection process by employing the previously selected aptamers for calmodulin (CaM) which includes a non-natural fluorogenic amino acid, 7-nitro-2,1,3-benzoxadiazole. RESULTS:We added five amino acids at the N-terminus which was employed for the selection and then we tested the affinity and selectivity for CaM binding. Surface plasmon resonance and fluorescence measurements showed that the additional amino acids for one of the aptamers drastically improved binding affinity to CaM, indicating the importance of aptamer use under the same conditions as the selection process. Such drastic improvement in affinity was not observed for the sequence which had been reported previously. Nuclear magnetic resonance data identified that the primary binding site is located in a C-terminal of CaM and the additional residues enhance interactions with CaM. CONCLUSIONS:We found that the addition of the common sequence, which was employed for ribosome display, makes the affinity of a selected peptide as strong as the previously reported peptide.
journal_name
Biotechnol Lettjournal_title
Biotechnology lettersauthors
Manandhar Y,Wang W,Inoue J,Hayashi N,Uzawa T,Ito Y,Aigaki T,Ito Ydoi
10.1007/s10529-016-2257-2subject
Has Abstractpub_date
2017-03-01 00:00:00pages
375-382issue
3eissn
0141-5492issn
1573-6776pii
10.1007/s10529-016-2257-2journal_volume
39pub_type
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