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^*

^*Autor correspondiente de este trabajo

Polytechnic University of Catalonia
University of California at San Diego
Belarus Academy of Sciences
University of California

Producción científica: Contribución a una revista › Artículo › revisión exhaustiva

9 Citas (Scopus)

Resumen

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.

Idioma original	Inglés
Páginas (desde-hasta)	264-268
Número de páginas	5
Publicación	Macromolecules
Volumen	28
N.º	1
DOI	https://doi.org/10.1021/ma00105a035
Estado	Publicada - 1 ene 1995
Publicado de forma externa	Sí

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

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.",

author = "V. Tereshko and X. Vidal and M. Goodman and Subirana, \{J. A.\}",

year = "1995",

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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

SN - 0024-9297

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SP - 264

EP - 268

JO - Macromolecules

JF - Macromolecules

IS - 1

ER -

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

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