Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency.

ABSTRACT: Recombinant proteins are important therapeutics due to potent, highly specific, and nontoxic actions in vivo. However, they are expensive medicines to manufacture, chemically unstable, and difficult to administer with low patient uptake and compliance. Small molecule drugs are cheaper and more bioavailable, but less target-specific in vivo and often have associated side effects. Here we combine some advantages of proteins and small molecules by taking short amino acid sequences that confer potency and selectivity to proteins, and fixing them as small constrained molecules that are chemically and structurally stable and easy to make. Proteins often use short alpha-helices of just 1-4 helical turns (4-15 amino acids) to interact with biological targets, but peptides this short usually have n

SUBMITTER: Harrison RS 

PROVIDER: S-EPMC2900680 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature