WETTABILITY AND MAIR INFRARED SPECTROSCOPY OF SOLVENT-CAST THIN FILMS OF POLYAMIDES AND POLYPEPTIDES.
Abstract
Polyamides, such as the nylons, polypeptides, and proteins, may have variable surface properties as the result of the masking or exposure of surface hydrogen-bonding sites which may greatly influence their behavior. An earlier investigation with the polyamide nylon 66, showing a wettability difference by hydrogen-bonding and nonhydrogen-bonding liquids, was confirmed and extended in the present work with nylon 11, nylon 6, and nylon 2 (polyglycine). This difference in wettability behavior seems diagnostic, when present in conjunction with a high critical-surface-tension range, for the presence of accessible amides in a polymer surface. Investigations of the more complex polypeptides, polymethylglutamate, and polybenzylglutamate by contact-angle determination and multiple attenuated internal reflection (MAIR) infrared spectroscopy on solvent-cast thin polymer films showed that the hydrogen-bonding capacity of the common polyamide backbone could be masked by either bulky side-chain substituents or by certain configuration changes of the polymer chain. Elimination of the hydrogen-bonding ability at nylon surfaces might also accompany polymer fractionation in different solvents, slight configuration changes, or a combination of both. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 16, 1968
- Accession Number
- AD0676888
Entities
People
- R. E. Baier
- William A. Zisman
Organizations
- United States Naval Research Laboratory