monopeptide

the monopeptide exhibited strong binding affinity to the receptor.

synthesis of the monopeptide was achieved using solid-phase peptide synthesis.

we designed a monopeptide to mimic a natural protein sequence.

the monopeptide's structure was analyzed by nmr spectroscopy.

the monopeptide demonstrated selective inhibition of the enzyme.

modifications to the monopeptide improved its stability in solution.

the monopeptide was conjugated to a carrier protein for enhanced immunogenicity.

we screened a library of monopeptides for potential drug candidates.

the monopeptide's biological activity was evaluated in vitro.

a cyclic monopeptide was synthesized to enhance proteolytic stability.

the monopeptide's sequence was optimized for improved cell permeability.