Self-Organization of Urea-Based Oligomers from Structure to Function

1 Introduction The remarkable and highly diverse biological activities exhibited by proteins rely on the unique capacity of these intrinsically flexible α-polypeptide chains to fold into well ordered and compact structures. The formation of protein tertiary and quaternary structures is attainable only with a small set of distinct secondary structural elements : i) sheets, ii) helices, and iii) turns.1IntroductionThe remarkable and highly diverse biological activities exhibited by proteins rel…     

Self-Organization of Urea-Based Oiigomers from Structure to Function

The remarkable and highly diverse biological activities exhibited by proteins rely on the unique capacity of these intrinsically flexible α-polypeptide chains to fold into well ordered and compact structures. The formation of protein tertiary and quaternary structures is attainable only with a small set of distinct secondary structural elements ： i） sheets, ii） helices, and iii） turns.     

Antimicrobial peptides: natural templates for synthetic membrane-active compounds

The innate immunity of multicellular organisms relies in large part on the action of antimicrobial peptides (AMPs) to resist microbial invasion. Crafted by evolution into an extremely diversified array of sequences and folds, AMPs do share a common amphiphilic 3-D arrangement. This feature is directly linked with a common mechanism of action that predominantly (although not exclusively) develops upon interaction of peptides with cell membranes of target cells. This minireview reports on current understanding of the modes of interaction of AMPs with biological and model membranes, especially focusing on recent insights into the folding and oligomerization requirements of peptides to bind and insert into lipid membranes and exert their antibiotic effects. Given the potential of AMPs to be developed into a new class of anti-infective agents, emphasis is placed on how the information on peptide-membrane interactions could direct the design and selection of improved biomimetic synthetic peptides with antibiotic properties.