Abstract
A synthetic human V(L) phage display library, created by the randomization of all complementarity-determining regions (CDRs) in a V(L) scaffold, was panned against three test antigens to determine the propensity of the library to yield non-aggregating binders. A total of 22 binders were isolated against the test antigens and the majority (20) were monomeric. Thus, human V(L) repertoires provide an efficient source of non-aggregating binders and represent an attractive alternative to human V(H) repertoires, which are notorious for containing high proportions of aggregating species. Moreover, the solubility of V(L)s, in contrast to V(H)s, appears much less CDR dependent.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Antibody Affinity
-
Antigens, Bacterial / genetics
-
Antigens, Bacterial / metabolism
-
Bacterial Proteins / genetics
-
Bacterial Proteins / metabolism
-
Bacterial Toxins / genetics
-
Bacterial Toxins / metabolism
-
Base Sequence
-
Cloning, Molecular
-
Enzyme-Linked Immunosorbent Assay
-
Humans
-
Immunoglobulin Light Chains / chemistry
-
Immunoglobulin Light Chains / genetics
-
Immunoglobulin Light Chains / metabolism*
-
Molecular Sequence Data
-
Peptide Library*
-
Protein Binding
-
Single-Chain Antibodies / chemistry
-
Single-Chain Antibodies / genetics
-
Single-Chain Antibodies / metabolism*
Substances
-
Antigens, Bacterial
-
Bacterial Proteins
-
Bacterial Toxins
-
Immunoglobulin Light Chains
-
Peptide Library
-
Single-Chain Antibodies
-
toxB protein, Clostridium difficile