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A Snake Venom Peptide and Its Derivatives Prevent Aß42 Aggregation and Eliminate Toxic Aß42 Aggregates In Vitro.
Camargo, Luana Cristina; Gering, Ian; Mastalipour, Mohammadamin; Kraemer-Schulien, Victoria; Bujnicki, Tuyen; Willbold, Dieter; Coronado, Mônika A; Eberle, Raphael J.
Afiliación
  • Camargo LC; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich 52428, Germany.
  • Gering I; Faculty of Mathematics and Natural Sciences, Institute of Physical Biology, Heinrich Heine University Düsseldorf, Düsseldorf 40225, Germany.
  • Mastalipour M; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich 52428, Germany.
  • Kraemer-Schulien V; Faculty of Mathematics and Natural Sciences, Institute of Physical Biology, Heinrich Heine University Düsseldorf, Düsseldorf 40225, Germany.
  • Bujnicki T; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich 52428, Germany.
  • Willbold D; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich 52428, Germany.
  • Coronado MA; Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich 52428, Germany.
  • Eberle RJ; Faculty of Mathematics and Natural Sciences, Institute of Physical Biology, Heinrich Heine University Düsseldorf, Düsseldorf 40225, Germany.
ACS Chem Neurosci ; 15(14): 2600-2611, 2024 Jul 17.
Article en En | MEDLINE | ID: mdl-38957957
ABSTRACT
Over a century has passed since Alois Alzheimer first described Alzheimer's disease (AD), and since then, researchers have made significant strides in understanding its pathology. One key feature of AD is the presence of amyloid-ß (Aß) peptides, which form amyloid plaques, and therefore, it is a primary target for treatment studies. Naturally occurring peptides have garnered attention for their potential pharmacological benefits, particularly in the central nervous system. In this study, nine peptide derivatives of Crotamine, a polypeptide from Crotalus durissus terrificus Rattlesnake venom, as well as one d-enantiomer, were evaluated for their ability to modulate Aß42 aggregation through various assays such as ThT, QIAD, SPR, and sFIDA. All tested peptides were able to decrease Aß42 aggregation and eliminate Aß42 aggregates. Additionally, all of the peptides showed an affinity for Aß42. This study is the first to describe the potential of crotamine derivative peptides against Aß42 aggregation and to identify a promising d-peptide that could be used as an effective pharmacological tool against AD in the future.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fragmentos de Péptidos / Péptidos beta-Amiloides / Venenos de Crotálidos Límite: Animals / Humans Idioma: En Revista: ACS Chem Neurosci Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fragmentos de Péptidos / Péptidos beta-Amiloides / Venenos de Crotálidos Límite: Animals / Humans Idioma: En Revista: ACS Chem Neurosci Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos