PubMed · 9229763
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I Williams. 1997-07-04. Drug development.. https://doi.org/10.1126/science.277.5322.17e
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The uptake and controlled release of model active substances from poly(ethylene oxide), (PEO), hydrogels synthesized by irradiation were investigated. For the characterization of network structure of PEO hydrogels, swelling properties in water and the number average molecular weight between crosslinks were determined. Salicylic acid, phthalic acid and resorcinol were used as model substances for their controlled release from PEO hydrogels. The effects of dose rate, total dose and chemical structure of active substance on the uptake and release have been studied. The active substance uptake capacity of hydrogels was found to be lowest for phthalic acid and highest for resorcinol in the gel system obtained by irradiation both at low and high dose rates. The release was lowest both in rate and in total amounts in hydrogels containing phthalic acid, more in those with salicylic acid and highest in those with resorcinol. The physical and chemical factors affecting the release of model compounds such as the network structure of hydrogels and hydrogen bond formation between the adsorbent and PEO chains were discussed.
beta-Peptides are a class of polyamides that have been demonstrated to adopt a variety of helical conformations. Recently, a series of amphiphilic L(+2) helical beta-peptides were designed, which were intended to mimic the overall physicochemical properties of a class of membrane-active antimicrobial peptides, including magainin and cecropin. Although these peptides showed potent antimicrobial activity, they also showed significant activity against human erythrocytes. Operating under the assumption that their lack of specificity arose from excessive hydrophobicity, two additional beta-peptides H-(beta(3)-HAla-beta(3)-HLys-beta(3)-HVal)(n)-NH(2) (n = 4, 5) were designed and synthesized. Both have high antimicrobial activities, but very low hemolytic potencies. The peptides bind in an L(+2) conformation to phospholipid vesicles, inducing leakage of entrapped small molecules. The peptides have a low affinity for membranes consisting of neutral phosphatidylcholine lipids, but bind avidly to vesicles containing 10 mol % of acidic phosphatidylserine lipids. Differences in vesicle leakage kinetics for the two peptides suggest that chain length could affect their mechanisms of disrupting cell membranes. Thus, insights gained from the study of variants of natural alpha-peptides have provided a useful guide for the design of nonnatural antimicrobial beta-peptides.
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