Skip to content
Licensed Unlicensed Requires Authentication Published by De Gruyter September 29, 2018

Fragment Aβ(18-41) presented within the CDR3 loop region of a shark immunoglobulin new antigen receptor single-variable domain antibody analyzed based on the fuzzy oil drop model

  • Mateusz Banach , Leszek Konieczny , Zdzisław Wiśniowski and Irena Roterman EMAIL logo

Abstract

The structure of amyloid Aβ(1-41) is the object of many papers due to the neurodegenerative processes induced by this amyloid. One of the ways to investigate the possible structural forms other than the amyloid is to incorporate the fragment of this peptide into the chain of immunoglobulin. Fragment Aβ(18-41) presented within the CDR3 loop region of a shark immunoglobulin new antigen receptor single-variable domain antibody is the object of this analysis. The structure of this hybrid is available in the PDB and analyzed based on the fuzzy oil drop model. The aim is to define the status of this fragment, revealing the possible fitting to the ordered form of the hydrophobic core. Simultaneously, the verification of the predisposition to complexation is possible.

Award Identifier / Grant number: K/ZDS/006363, K/ZDS/006366

Funding statement: Uniwersytet Jagielloński Collegium Medicum, Funder Id: 10.13039/100009045, Grant Number: K/ZDS/006363, K/ZDS/006366.

  1. Author contributions: The authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Employment or leadership: None declared.

  3. Honorarium: None declared.

  4. Competing interests: The funding organization(s) played no role in the study design; in the collection, analysis, and interpretation of data; in the writing of the report; or in the decision to submit the report for publication.

References

[1] Berchtold NC, Cotman CW. Evolution in the conceptualization of dementia and Alzheimer’s disease: Greco-Roman period to the 1960s. Neurobiol Aging 1998;19:173–89.10.1016/S0197-4580(98)00052-9Search in Google Scholar PubMed

[2] Brookmeyer R, Gray S, Kawas C. Projections of Alzheimer’s disease in the United States and the public health impact of delaying disease onset. Am J Public Health 1998;88:1337–42.10.2105/AJPH.88.9.1337Search in Google Scholar PubMed

[3] Brookmeyer R, Johnson E, Ziegler-Graham K, Arrighi MH, Johnson E, Ziegler-Graham K, Arrighi HM. Forecasting the global burden of Alzheimer’s disease. Alzheimers Dementia 2007;3:186–91.10.1016/j.jalz.2007.04.381Search in Google Scholar PubMed

[4] Streltsov VA, Varghese JN, Masters CL, Nuttall SD. Crystal structure of the amyloid-β p3 fragment provides a model for oligomer formation in Alzheimer’s disease. J Neurosci 2011;31:1419–26.10.1523/JNEUROSCI.4259-10.2011Search in Google Scholar PubMed PubMed Central

[5] Tycko R. Indirect detection in solid state NMR: an illustrious history and a bright future. J Magn Reson 2018;288:122–3.10.1016/j.jmr.2018.02.014Search in Google Scholar PubMed PubMed Central

[6] Tycko R. Alzheimer’s disease: structure of aggregates revealed. Nature 2016;537:492–3.10.1038/nature19470Search in Google Scholar PubMed PubMed Central

[7] Kalinowska B, Banach M, Konieczny L, Roterman I. Application of divergence entropy to characterize the structure of the hydrophobic core in DNA interacting proteins. Entropy 2015;17:1477–507.10.3390/e17031477Search in Google Scholar

[8] Kullback S, Leibler RA. On information and sufficiency. Ann Math Stat 1951;22:79–86.10.1214/aoms/1177729694Search in Google Scholar

[9] Dułak D, Banach M, Gadzała M, Konieczny L, Roterman I. Structural analysis of the Aβ(15-40) amyloid fibrils. Submitted for publication.Search in Google Scholar

[10] Dułak D, Banach M, Gadzała M, Konieczny L, Roterman I. Structural analysis of Aβ(1-40) amyloid. Submitted for publication.Search in Google Scholar

[11] Dułak D, Banach M, Gadzała M, Konieczny L, Roterman I. Structural analysis of Aβ(11-42) amyloid. Submitted for publication.Search in Google Scholar

Received: 2018-08-24
Accepted: 2018-09-14
Published Online: 2018-09-29

©2018 Walter de Gruyter GmbH, Berlin/Boston

Downloaded on 2.5.2024 from https://www.degruyter.com/document/doi/10.1515/bams-2018-0028/html
Scroll to top button