Selecting HIV-gp 120 binders by affinity in a microfluidic device

A. PEÑAHERRERA; JL.TORÁN; J. CASASNOVAS; A. VACA; G. ROSERO; M. PÉREZ; BETIANA LERNER

Heidelberg

Congreso; Microfluidics EMBL; 2018

Smith & Petrenko (1985) envisioned an artificial chemical evolution that links a protein with the genetic machinery that encodes it [1]. Peptide librariesare constructed fusing ramdomly-generated peptides to phage coat proteins and library panning promotes specific phage clones to be enriched on the basis of their affinity for a ligand [2]. Therefore, relatively rare ligand-bindingclones can be rapidly and efficiently rescued from large libraries. As panning is a laborious procedure, microfluidics offers a platform that enhancesstochastic encounters between phages and antigens in the controlled fluidic environment [3]. In this study, antibodies against HIV-gp 120 [4] havebeen displayed in M13 phage to be injected in a 1% agarose gel that has been functionalized with gp 120 protein to select phages that interact with itaccording to their affinity.