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Biomedical subjects

K W Funk

Publications and source records attributed to K W Funk.

4 recordsLinked to original sources
PubMed2000

Total synthesis and antifungal evaluation of cyclic aminohexapeptides.

The need for new therapies to treat systemic fungal infections continues to rise. Naturally occurring hexapeptide echinocandin B (1) has shown potent antifungal activity via its inhibition of the synthesis of beta-1,3 glucan, a key fungal cell wall component. Although this series of agents has been limited thus far based on their physicochemical characteristics, we have found that the synthesis of analogues bearing an aminoproline residue in the 'northwest' position imparts greatly improved water solubility (> 5 mg/mL). The synthesis and structure-activity relationships (SAR) based on whole cell and upon in vivo activity of the series of compounds are reported.

Acute Disease↗
PubMed1998

LHRH agonists.

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Animals↗
PubMed1976

A re-examination of the conformation of secretin in water.

An examination of a series of peptides corresponding to partial sequences of secretin and the application of empirical conformational parameters to the sequence has reopened the question about the position of the short helical stretch in the folded chain. In earlier studies, this was tentatively placed near the N-terminus, while newly accumulated evidence points to the C-terminal area. The possible role of ion pairs in the stabilization of the folding was investigated by the preparation and examination of synthetic analogues of the C-terminal tricosapeptide part of secretin. The carboxyl groups of glutamic acid (in position 9) and of aspartic acid (in position 15) were replaced by carboxamides. The 9-glutamine and the 15-asparagine analogues show a significant decrease in helical character. This loss of "structure" is even more pronounced in the 9-glutamine-15-asparagine tricosapeptide. Thus, ion-pair formation is indeed implicated as one of the forces which stabilize the folded conformation of the chain. Possible correlations between biological activity and secretin-like architecture were studied on several smooth muscle preparations.

Amino Acid Sequence↗