Premium
Making sense from antisense: A review of experimental data and developing ideas on sense–antisense peptide recognition
Author(s) -
Tropsha Alexander,
Kizer John S.,
Chaiken Irwin M.
Publication year - 1992
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300050202
Subject(s) - sense (electronics) , peptide , molecular recognition , folding (dsp implementation) , amphiphile , sense strand , computational biology , chemistry , antisense therapy , combinatorial chemistry , biochemistry , biology , dna , rna , oligonucleotide , gene , polymer , molecule , copolymer , organic chemistry , electrical engineering , engineering , locked nucleic acid
Peptides encoded in the antisense strand of DNA have been predicted and found experimentally to bind to sense peptides and proteins with significant selectivity and affinity. Such sense–antisense peptide recognition has been observed in many systems, most often by detecting binding between immobilized and soluble interaction partners. Data obtained so far on sequence and solvent dependence of interaction support a hydrophobic‐hydrophilic (amphipathic) model of peptide recognition. Nonetheless, the mechanistic understanding of this type of molecular recognition remains incomplete. Improving this understanding likely will require expanding the types of characteristics measured for sense–antisense peptide complexes and hence the types of analytical methods applied to such interactions. Understanding the mechanism of sense–antisense peptide recognition also may provide insights into mechanisms of native (sense) peptide and protein interactions and protein folding. Such insight may be helpful to learn how to design macromolecular recognition agents in technology for separation, diagnostics and therapeutics.