coiled 
 coils are a major motif in proteins and orchestrate multimerization 
 of various complexes important for biological processes . 
 inhibition 
 of coiled coil - mediated interactions has significant biomedical 
 potential . 
 however , general approaches that afford short peptides 
 with defined coiled coil conformation remain elusive . 
 we evaluated 
 several strategies to stabilize minimal helical bundles , with the 
 dimer motif as the initial focus . 
 a stable dimeric scaffold was realized 
 in a synthetic sequence by replacing an interhelical ionic bond 
 with a covalent bond . 
 application of this strategy to a more challenging 
 native protein  protein interaction ( ppi ) suggested that 
 an additional constraint , a disulfide bond at the internal a / d position along with a linker 
 at the e / e position , is 
 required for enhanced conformational stability . 
 we anticipate the 
 coiled coil stabilization methodology described herein to yield new 
 classes of modulators for ppis .