Influence of different tripeptides on the stability of the collagen triple helix. I. Analysis of the collagen sequence and identification of typical tripeptides

Biopolymers ◽  
1986 ◽  
Vol 25 (6) ◽  
pp. 1069-1080 ◽  
Author(s):  
R. Dölz ◽  
E. Heidemann
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix ◽  
The Stability

Different Effects of 4-Hydroxyproline and 4-Fluoroproline on the Stability of Collagen Triple Helix

Biochemistry ◽  
2005 ◽  
Vol 44 (16) ◽  
pp. 6034-6042 ◽  
Author(s):  
Yoshinori Nishi ◽  
Susumu Uchiyama ◽  
Masamitsu Doi ◽  
Yuji Nishiuchi ◽  
Takashi Nakazawa ◽  
...  
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix ◽  
The Stability

scholarly journals Contribution of dipole-dipole interactions to the stability of the collagen triple helix

2008 ◽  
Vol 17 (5) ◽  
pp. 955-961 ◽  
Author(s):  
Roberto Improta ◽  
Rita Berisio ◽  
Luigi Vitagliano
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix ◽  
Dipole Interactions ◽  
The Stability

Influences on the stability of collagen triple-helix

2014 ◽  
Vol 362 ◽  
pp. 113-117 ◽  
Author(s):  
Sabine Schweizer ◽  
Andreas Bick ◽  
Lalitha Subramanian ◽  
Xenophon Krokidis
Keyword(s):  
Triple Helix ◽  
Collagen Triple Helix ◽  
The Stability

Effect of N- and C-terminal functional groups on the stability of collagen triple helices

2017 ◽  
Vol 53 (80) ◽  
pp. 11036-11039 ◽  
Author(s):  
Jasmine Egli ◽  
Roman S. Erdmann ◽  
Pascal J. Schmidt ◽  
Helma Wennemers
Keyword(s):  
Functional Groups ◽  
Triple Helix ◽  
Collagen Triple Helix ◽  
Triple Helices ◽  
The Stability

The effect of chargedversusneutral N- and C-termini on the stability of the collagen triple helix was examined.

A THEORETICAL STUDY OF THE SUBSTITUENT EFFECT ON THE STABILITY OF COLLAGEN

2004 ◽  
Vol 03 (02) ◽  
pp. 225-243 ◽  
Author(s):  
JUN-MIN QUAN ◽  
YUN-DONG Wu
Keyword(s):  
Electrostatic Interactions ◽  
Triple Helix ◽  
Density Functional ◽  
Theoretical Calculations ◽  
Substituent Effects ◽  
Binding Energies ◽  
Model Studies ◽  
Collagen Triple Helix ◽  
Triple Helices ◽  
The Stability

Theoretical calculations have been carried out to investigate the effect of the 4(R)-substituents ( OH , F , NH 2, and [Formula: see text]) in proline on the stability of the collagen triple helix. A series of substituted proline models were studied first with density functional (B3LYP/6-31+G*) calculations. The solvent effect was studied using the SCIPCM method. While the F , OH and NH 2 groups increase the stability of the trans-up conformation with respect to the trans-down conformation, [Formula: see text] appears to favor the trans-down conformation in an aqueous solution. Second, the triple helices of the tripeptide models, Ac – Pro – Pro(X) – Gly – H with the two proline residues in the down/down and down/up puckering conformations, were optimized with a repeating unit approach using the HF/6-31G* method. For the Ac – Pro – Pro – Gly – H model peptide, the calculated binding energies of the two triple helices with the different puckering modes are similar. All four substituents, F , OH , NH 2, and [Formula: see text], considerably increased the binding energy of the down/up helix, but only [Formula: see text] stabilizes the down/down triple helix. Our calculations indicate that the inter-chain electrostatic interactions involving the 4(R)-substituents play an important role in stabilizing triple helical collagen models and allow the rationalization of all available experimental observations. Further model studies indicate that the substituent effects by the F , OH and NH 2 substituents are local while the effect of [Formula: see text] is long-range in nature.

scholarly journals The Role of Collagen Triple Helix Repeat-Containing 1 Protein (CTHRC1) in Rheumatoid Arthritis

2021 ◽  
Vol 22 (5) ◽  
pp. 2426
Author(s):  
Askhat Myngbay ◽  
Limara Manarbek ◽  
Steve Ludbrook ◽  
Jeannette Kunz
Keyword(s):  
Rheumatoid Arthritis ◽  
Drug Targets ◽  
Triple Helix ◽  
Cancer Metastasis ◽  
Bone Erosion ◽  
Cartilage Destruction ◽  
Patient Treatment ◽  
Collagen Triple Helix ◽  
Potential Biomarker

Rheumatoid arthritis (RA) is a chronic autoimmune disease causing inflammation of joints, cartilage destruction and bone erosion. Biomarkers and new drug targets are actively sought and progressed to improve available options for patient treatment. The Collagen Triple Helix Repeat Containing 1 protein (CTHRC1) may have an important role as a biomarker for rheumatoid arthritis, as CTHRC1 protein concentration is significantly elevated in the peripheral blood of rheumatoid arthritis patients compared to osteoarthritis (OA) patients and healthy individuals. CTHRC1 is a secreted glycoprotein that promotes cell migration and has been implicated in arterial tissue-repair processes. Furthermore, high CTHRC1 expression is observed in many types of cancer and is associated with cancer metastasis to the bone and poor patient prognosis. However, the function of CTHRC1 in RA is still largely undefined. The aim of this review is to summarize recent findings on the role of CTHRC1 as a potential biomarker and pathogenic driver of RA progression. We will discuss emerging evidence linking CTHRC1 to the pathogenic behavior of fibroblast-like synoviocytes and to cartilage and bone erosion through modulation of the balance between bone resorption and repair.

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