Bae, Hyung Eun Jung, Jaeyong Sung, Jeong Soo Kwon, Soonil Kang, Min-Jung Jose, Joachim Pyun, Jae-Chul 2025-05-22T06:31:35Z 2025-05-22T06:31:35Z 2025-05-21 2025-06 2050-750X https://pubs.kist.re.kr/handle/201004/152500 A penicillin-like mimotope was screened from an Fv-antibody library which had the inhibition activity of beta-lactamase. Fv-antibody indicated the variable region (VH) of the immunoglobulin G, which includes three complementarity determining regions (CDRs). The Fv-antibody library was then prepared by randomizing the complementarity determining region 3 (CDR3), and it was expressed on the outer membrane of E. coli. The penicillin-like mimotopes were screened from the Fv-antibody library using magnetic beads with an immobilized monoclonal anti-penicillin antibody. The screened mimotopes were expressed as soluble Fv-antibodies and were also synthesized into peptides (11-mer). The binding affinity (KD) of the expressed Fv-antibodies and synthesized peptides was estimated using SPR measurements. The beta-lactamase inhibition activity of the Fv-antibodies and synthetic peptides was estimated using colorimetry based on the formation of penicilloic acid. The penicillin-like mimotopes of the expressed Fv-antibodies and synthesized peptides were demonstrated to have beta-lactamase inhibition activity in the bacterial lysates. Finally, the docking analysis of beta-lactamase and the screened CDR3 sequences demonstrated that the screened CDR3 sequences were specifically bound to the binding sites of beta-lactamase. English Royal Society of Chemistry Penicillin-like mimotopes from autodisplayed Fv-antibody library inhibiting β-lactamase activity Article 10.1039/d4tb02793k 1 Journal of Materials Chemistry B, v.13, no.21, pp.6154 - 6163 Journal of Materials Chemistry B 13 21 6154 6163 Y scie scopus 001481616000001 2-s2.0-105004907331 Materials Science, Biomaterials Materials Science Article DOCKING ACID SURFACE-PLASMON RESONANCE ESCHERICHIA-COLI ASSAY BINDING CDR3 ANTIBIOTICS RESISTANCE DIVERSITY