Effects of disulfide bond and cholesterol derivatives on human calcitonin amyloid formation

Biopolymers ◽  
2019 ◽  
Vol 111 (5) ◽  
Author(s):  
Richard Lantz ◽  
Brian Busbee ◽  
Ewa P. Wojcikiewicz ◽  
Deguo Du
Keyword(s):  
Disulfide Bond ◽  
Human Calcitonin ◽  
Amyloid Formation

scholarly journals Elucidating the Role of Disulfide Bond on Amyloid Formation and Fibril Reversibility of Somatostatin-14

2014 ◽  
Vol 289 (24) ◽  
pp. 16884-16903 ◽  
Author(s):  
Arunagiri Anoop ◽  
Srivastav Ranganathan ◽  
Bhagwan Das Dhaked ◽  
Narendra Nath Jha ◽  
Supriya Pratihar ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Amyloid Formation ◽  
Somatostatin 14

Flavonoids with Vicinal Hydroxyl Groups Inhibit Human Calcitonin Amyloid Formation

2020 ◽  
Vol 26 (57) ◽  
pp. 13063-13071
Author(s):  
Richard Lantz ◽  
Brian Busbee ◽  
Ewa P. Wojcikiewicz ◽  
Deguo Du
Keyword(s):  
Hydroxyl Groups ◽  
Human Calcitonin ◽  
Amyloid Formation

scholarly journals Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Lynn Radamaker ◽  
Sara Karimi-Farsijani ◽  
Giada Andreotti ◽  
Julian Baur ◽  
Matthias Neumann ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Germ Line ◽  
Somatic Hypermutation ◽  
Ex Vivo ◽  
The Body ◽  
Al Amyloidosis ◽  
Amyloid Formation ◽  
Post Translational Modifications ◽  
Fibril Morphology ◽  
Al Amyloid

AbstractSystemic AL amyloidosis is a rare disease that is caused by the misfolding of immunoglobulin light chains (LCs). Potential drivers of amyloid formation in this disease are post-translational modifications (PTMs) and the mutational changes that are inserted into the LCs by somatic hypermutation. Here we present the cryo electron microscopy (cryo-EM) structure of an ex vivo λ1-AL amyloid fibril whose deposits disrupt the ordered cardiomyocyte structure in the heart. The fibril protein contains six mutational changes compared to the germ line and three PTMs (disulfide bond, N-glycosylation and pyroglutamylation). Our data imply that the disulfide bond, glycosylation and mutational changes contribute to determining the fibril protein fold and help to generate a fibril morphology that is able to withstand proteolytic degradation inside the body.

Synthesis of the amino-terminal decapeptide of human calcitonin, in which the disulfide bond is replaced by a thioether group

1980 ◽  
Vol 45 (4) ◽  
pp. 1305-1314 ◽  
Author(s):  
Zdenko Procházka ◽  
Karel Jošt
Keyword(s):  
Disulfide Bond ◽  
Human Calcitonin ◽  
Amino Terminal ◽  
Active Ester ◽  
Stepwise Method ◽  
Group A

A fully protected amino-terminal decapeptide Ib with the sequence of human calcitonin, in which the S-S bridge was replaced by the S-CH2 group (a so-called 7-carba-analogue), was synthetized mainly by the stepwise method. The cyclization of the linear decapeptide was performed by means of active ester.

Effects of a disulfide bridge prior to amyloid formation of the ABRI peptide

RSC Advances ◽  
2014 ◽  
Vol 4 (70) ◽  
pp. 36923-36928 ◽  
Author(s):  
Jorge A. Ceballos ◽  
Marco A. Giraldo ◽  
Pilar Cossio
Keyword(s):  
Surface Area ◽  
Disulfide Bond ◽  
Hydrophobic Surface ◽  
Disulfide Bridge ◽  
Amyloid Formation ◽  
Computational Studies

Computational studies characterize remarkable differences between the most probable structures of the monomeric amyloidogenic peptide, ABRI, with and without a single disulfide bond; the peptide is compact and alpha-helical with the bond, otherwise it is partially extended with slight β-bridges and an exposed hydrophobic surface area.

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