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

• Autorzy: Banach M. , Konieczny L. , Wiśniowski Z. , Roterman I.

Identyfikatory

DOI

10.1515/bams-2018-0028

• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

amyloid Aβ(1-41); hydrophobicity; immunoglobulin variable domain

• Wydawca: Uniwersytet Jagielloński - Collegium Medicum ; De Gruyter
• Czasopismo: Bio-Algorithms and Med-Systems
• Rocznik: 2018
• Tom: Vol. 14, no. 3
• Strony: art. no. 20180028
• Opis fizyczny: Bibliogr. 11 poz., rys., tab.

Twórcy

autor

Banach M.

• Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, 31-530 Krakow, Łazarza 16, Krakow, Poland

autor

Konieczny L.

• Chair of Medical Biochemistry, Jagiellonian University Medical College, 31-034 Krakow, Kopernika 7, Krakow, Poland

autor

Wiśniowski Z.

• Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, 31-530 Krakow, Łazarza 16, Krakow, Poland

autor

Roterman I.

• Department of Bioinformatics and Telemedicine, Jagiellonian University Medical College, 31-530 Krakow, Łazarza 16, Krakow, Poland

Bibliografia

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• [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.
• [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.
• [5] Tycko R. Indirect detection in solid state NMR: an illustrious history and a bright future. J Magn Reson 2018;288:122-3.
• [6] Tycko R. Alzheimer’s disease: structure of aggregates revealed. Nature 2016;537:492-3.
• [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.
• [8] Kullback S, Leibler RA. On information and sufficiency. Ann Math Stat 1951;22:79-86.
• [9] Dułak D, Banach M, Gadzała M, Konieczny L, Roterman I. Structural analysis of the Aβ(15-40) amyloid fibrils. Submitted for publication.
• [10] Dułak D, Banach M, Gadzała M, Konieczny L, Roterman I. Structural analysis of Aβ(1-40) amyloid. Submitted for publication.
• [11] Dułak D, Banach M, Gadzała M, Konieczny L, Roterman I. Structural analysis of Aβ(11-42) amyloid. Submitted for publication.

Uwagi

Opracowanie rekordu w ramach umowy 509/P-DUN/2018 ze środków MNiSW przeznaczonych na działalność upowszechniającą naukę (2019).