Structure of Oligomers of Glycine and e-Aminocaproic Acid as a Model of Nylon 2/6

V. Tereshko; X. Vidal; M. Goodman; J. A. Subirana

doi:10.1021/ma00105a035

Structure of Oligomers of Glycine and e-Aminocaproic Acid as a Model of Nylon 2/6

V. Tereshko
, X. Vidal
, M. Goodman
, J. A. Subirana^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

9 Citations (Scopus)

Abstract

We have determined the structure of acetyl-(glycyl-∈-aminocaproyl)₂-NH-propyl by X-ray diffraction methods as a model of nylon 2/6. The structure obtained confirms the tendency of glycine copolyamides to adopt a structure similar to polyglycine II with hydrogen bonds in three different directions. Our results also show that the ∈-aminocaproyl residue adopts a conformation in which its two terminal peptide groups form hydrogen bonds with an angle of about 120°. This observation might be of interest in order to understand the polymorphism of nylon 6.

Original language	English
Pages (from-to)	264-268
Number of pages	5
Journal	Macromolecules
Volume	28
Issue number	1
DOIs	https://doi.org/10.1021/ma00105a035
Publication status	Published - 1 Jan 1995
Externally published	Yes

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abstract = "We have determined the structure of acetyl-(glycyl-∈-aminocaproyl)2-NH-propyl by X-ray diffraction methods as a model of nylon 2/6. The structure obtained confirms the tendency of glycine copolyamides to adopt a structure similar to polyglycine II with hydrogen bonds in three different directions. Our results also show that the ∈-aminocaproyl residue adopts a conformation in which its two terminal peptide groups form hydrogen bonds with an angle of about 120°. This observation might be of interest in order to understand the polymorphism of nylon 6.",

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T1 - Structure of Oligomers of Glycine and e-Aminocaproic Acid as a Model of Nylon 2/6

AU - Tereshko, V.

AU - Vidal, X.

AU - Goodman, M.

AU - Subirana, J. A.

PY - 1995/1/1

Y1 - 1995/1/1

N2 - We have determined the structure of acetyl-(glycyl-∈-aminocaproyl)2-NH-propyl by X-ray diffraction methods as a model of nylon 2/6. The structure obtained confirms the tendency of glycine copolyamides to adopt a structure similar to polyglycine II with hydrogen bonds in three different directions. Our results also show that the ∈-aminocaproyl residue adopts a conformation in which its two terminal peptide groups form hydrogen bonds with an angle of about 120°. This observation might be of interest in order to understand the polymorphism of nylon 6.

AB - We have determined the structure of acetyl-(glycyl-∈-aminocaproyl)2-NH-propyl by X-ray diffraction methods as a model of nylon 2/6. The structure obtained confirms the tendency of glycine copolyamides to adopt a structure similar to polyglycine II with hydrogen bonds in three different directions. Our results also show that the ∈-aminocaproyl residue adopts a conformation in which its two terminal peptide groups form hydrogen bonds with an angle of about 120°. This observation might be of interest in order to understand the polymorphism of nylon 6.

UR - https://www.scopus.com/pages/publications/0029632225

U2 - 10.1021/ma00105a035

DO - 10.1021/ma00105a035

M3 - Article

AN - SCOPUS:0029632225

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JO - Macromolecules

JF - Macromolecules

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ER -

Structure of Oligomers of Glycine and e-Aminocaproic Acid as a Model of Nylon 2/6

Abstract

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