izpis_h1_title_alt

Amyloid fibrils of stefin B show anisotropic properties
ID Žganec, Matjaž (Avtor), ID Taler-Verčič, Ajda (Avtor), ID Muševič, Igor (Avtor), ID Škarabot, Miha (Avtor), ID Žerovnik, Eva (Avtor)

.pdfPDF - Predstavitvena datoteka, prenos (2,38 MB)
MD5: A4219990861F41B1A614153271DBA1B1
URLURL - Izvorni URL, za dostop obiščite https://www.mdpi.com/1422-0067/24/4/3737 Povezava se odpre v novem oknu

Izvleček
Human stefin B, a member of the cystatin family of cysteine protease inhibitors, tends to form amyloid fibrils under relatively mild conditions, which is why it is used as a model protein to study amyloid fibrillation. Here, we show for the first time that bundles of amyloid fibrils, i.e., helically twisted ribbons, formed by human stefin B exhibit birefringence. This physical property is commonly observed in amyloid fibrils when stained with Congo red. However, we show that the fibrils arrange in regular anisotropic arrays and no staining is required. They share this property with anisotropic protein crystals, structured protein arrays such as tubulin and myosin, and other anisotropic elongated materials, such as textile fibres and liquid crystals. In certain macroscopic arrangements of amyloid fibrils, not only birefringence is observed, but also enhanced emission of intrinsic fluorescence, implying a possibility to detect amyloid fibrils with no labels by using optical microscopy. In our case, no enhancement of intrinsic tyrosine fluorescence was observed at 303 nm; instead, an additional fluorescence emission peak appeared at 425 to 430 nm. We believe that both phenomena, birefringence and fluorescence emission in the deep blue, should be further explored with this and other amyloidogenic proteins. This may allow the development of label-free detection methods for amyloid fibrils of different origins.

Jezik:Angleški jezik
Ključne besede:nano-sized object, bundle of amyloid fibrils, birefringence, intrinsic fluorescence, label-free imaging
Vrsta gradiva:Članek v reviji
Tipologija:1.01 - Izvirni znanstveni članek
Organizacija:FMF - Fakulteta za matematiko in fiziko
MF - Medicinska fakulteta
Status publikacije:Objavljeno
Različica publikacije:Objavljena publikacija
Leto izida:2023
Št. strani:10 str.
Številčenje:Vol. 24, iss. 4, art. 3737
PID:20.500.12556/RUL-155598 Povezava se odpre v novem oknu
UDK:577.112
ISSN pri članku:1661-6596
DOI:10.3390/ijms24043737 Povezava se odpre v novem oknu
COBISS.SI-ID:142086659 Povezava se odpre v novem oknu
Datum objave v RUL:08.04.2024
Število ogledov:337
Število prenosov:78
Metapodatki:XML DC-XML DC-RDF
:
Kopiraj citat
Objavi na:Bookmark and Share

Gradivo je del revije

Naslov:International journal of molecular sciences
Skrajšan naslov:Int. j. mol. sci.
Založnik:MDPI
ISSN:1661-6596
COBISS.SI-ID:36217605 Povezava se odpre v novem oknu

Licence

Licenca:CC BY 4.0, Creative Commons Priznanje avtorstva 4.0 Mednarodna
Povezava:http://creativecommons.org/licenses/by/4.0/deed.sl
Opis:To je standardna licenca Creative Commons, ki daje uporabnikom največ možnosti za nadaljnjo uporabo dela, pri čemer morajo navesti avtorja.

Sekundarni jezik

Jezik:Slovenski jezik
Ključne besede:delci nanovelikosti, skupki amiloidnih fibril, dvolomnost, intrinzična fluorescenca, slikanje brez označevanja

Projekti

Financer:ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Številka projekta:J7-4050
Naslov:Oligomeri amiloidogenih proteinov od a do ž; biofizikalne lastnosti, struktura, funkcija in medsebojne interakcije

Financer:ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Številka projekta:P1-0140
Naslov:Proteoliza in njena regulacija pri zdravju in boleznih

Podobna dela

Podobna dela v RUL:
Podobna dela v drugih slovenskih zbirkah:

Nazaj