Aarhus University Seal / Aarhus Universitets segl

Zhefei Zhang

Photodegradation of porphyrin-bound hIAPP(1-37) fibrils

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

Photodegradation of porphyrin-bound hIAPP(1-37) fibrils. / Song, Yongxiu; Li, Ping; Zhang, Zhiming; Wang, Yin; Zhang, Zhefei; Liu, Lei; Dong, Mingdong.

In: New Journal of Chemistry, Vol. 44, No. 22, 06.2020, p. 9438-9443.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Song, Y, Li, P, Zhang, Z, Wang, Y, Zhang, Z, Liu, L & Dong, M 2020, 'Photodegradation of porphyrin-bound hIAPP(1-37) fibrils', New Journal of Chemistry, vol. 44, no. 22, pp. 9438-9443. https://doi.org/10.1039/c9nj06082k

APA

Song, Y., Li, P., Zhang, Z., Wang, Y., Zhang, Z., Liu, L., & Dong, M. (2020). Photodegradation of porphyrin-bound hIAPP(1-37) fibrils. New Journal of Chemistry, 44(22), 9438-9443. https://doi.org/10.1039/c9nj06082k

CBE

Song Y, Li P, Zhang Z, Wang Y, Zhang Z, Liu L, Dong M. 2020. Photodegradation of porphyrin-bound hIAPP(1-37) fibrils. New Journal of Chemistry. 44(22):9438-9443. https://doi.org/10.1039/c9nj06082k

MLA

Song, Yongxiu et al. "Photodegradation of porphyrin-bound hIAPP(1-37) fibrils". New Journal of Chemistry. 2020, 44(22). 9438-9443. https://doi.org/10.1039/c9nj06082k

Vancouver

Song Y, Li P, Zhang Z, Wang Y, Zhang Z, Liu L et al. Photodegradation of porphyrin-bound hIAPP(1-37) fibrils. New Journal of Chemistry. 2020 Jun;44(22):9438-9443. https://doi.org/10.1039/c9nj06082k

Author

Song, Yongxiu ; Li, Ping ; Zhang, Zhiming ; Wang, Yin ; Zhang, Zhefei ; Liu, Lei ; Dong, Mingdong. / Photodegradation of porphyrin-bound hIAPP(1-37) fibrils. In: New Journal of Chemistry. 2020 ; Vol. 44, No. 22. pp. 9438-9443.

Bibtex

@article{71cdd62ecf9d4f94a786cff42213bc08,
title = "Photodegradation of porphyrin-bound hIAPP(1-37) fibrils",
abstract = "Amyloid deposits in pancreatic islets of type 2 diabetes mellitus (T2DM) are mainly comprised of human islet amyloid polypeptide (hIAPP), which is believed to be generated as a paracrine hormone along with insulin secretion. Misfolded hIAPP in islet beta cells is associated with T2DM. To reduce the risk of T2DM, amyloid aggregate degradation to remove insoluble amyloid deposits has been proven to be a preventive strategy against T2DM. However, the development of effective approaches and degradation mechanisms needs to be further addressed. Herein, we introduce tetrasodium-meso-tetra(4-sulfonatophenyl)porphyrin binding to hIAPP37 aggregates by electrostatic interactions, which could enhance the degradability of hIAPP37 fibrils under photo-irradiation. The morphology change of hIAPP fibrils could be easily revealed through the effect of photoexcited porphyrin without any additives under neutral conditions. The photoexcited porphyrin-induced degradation of amyloid fibrils may be attributed to reactive oxygen species destabilizing the β-sheet secondary structure under photo-irradiation. Moreover, the degraded products of hIAPP37 fibrils show low cytotoxicity to INS cells. This work could be beneficial for the molecular design of novel photodegradation agents of amyloid fibrils and also expand the biomedical application of porphyrin for photosensitization.",
author = "Yongxiu Song and Ping Li and Zhiming Zhang and Yin Wang and Zhefei Zhang and Lei Liu and Mingdong Dong",
year = "2020",
month = jun,
doi = "10.1039/c9nj06082k",
language = "English",
volume = "44",
pages = "9438--9443",
journal = "New Journal of Chemistry",
issn = "1144-0546",
publisher = "ROYAL SOC CHEMISTRY",
number = "22",

}

RIS

TY - JOUR

T1 - Photodegradation of porphyrin-bound hIAPP(1-37) fibrils

AU - Song, Yongxiu

AU - Li, Ping

AU - Zhang, Zhiming

AU - Wang, Yin

AU - Zhang, Zhefei

AU - Liu, Lei

AU - Dong, Mingdong

PY - 2020/6

Y1 - 2020/6

N2 - Amyloid deposits in pancreatic islets of type 2 diabetes mellitus (T2DM) are mainly comprised of human islet amyloid polypeptide (hIAPP), which is believed to be generated as a paracrine hormone along with insulin secretion. Misfolded hIAPP in islet beta cells is associated with T2DM. To reduce the risk of T2DM, amyloid aggregate degradation to remove insoluble amyloid deposits has been proven to be a preventive strategy against T2DM. However, the development of effective approaches and degradation mechanisms needs to be further addressed. Herein, we introduce tetrasodium-meso-tetra(4-sulfonatophenyl)porphyrin binding to hIAPP37 aggregates by electrostatic interactions, which could enhance the degradability of hIAPP37 fibrils under photo-irradiation. The morphology change of hIAPP fibrils could be easily revealed through the effect of photoexcited porphyrin without any additives under neutral conditions. The photoexcited porphyrin-induced degradation of amyloid fibrils may be attributed to reactive oxygen species destabilizing the β-sheet secondary structure under photo-irradiation. Moreover, the degraded products of hIAPP37 fibrils show low cytotoxicity to INS cells. This work could be beneficial for the molecular design of novel photodegradation agents of amyloid fibrils and also expand the biomedical application of porphyrin for photosensitization.

AB - Amyloid deposits in pancreatic islets of type 2 diabetes mellitus (T2DM) are mainly comprised of human islet amyloid polypeptide (hIAPP), which is believed to be generated as a paracrine hormone along with insulin secretion. Misfolded hIAPP in islet beta cells is associated with T2DM. To reduce the risk of T2DM, amyloid aggregate degradation to remove insoluble amyloid deposits has been proven to be a preventive strategy against T2DM. However, the development of effective approaches and degradation mechanisms needs to be further addressed. Herein, we introduce tetrasodium-meso-tetra(4-sulfonatophenyl)porphyrin binding to hIAPP37 aggregates by electrostatic interactions, which could enhance the degradability of hIAPP37 fibrils under photo-irradiation. The morphology change of hIAPP fibrils could be easily revealed through the effect of photoexcited porphyrin without any additives under neutral conditions. The photoexcited porphyrin-induced degradation of amyloid fibrils may be attributed to reactive oxygen species destabilizing the β-sheet secondary structure under photo-irradiation. Moreover, the degraded products of hIAPP37 fibrils show low cytotoxicity to INS cells. This work could be beneficial for the molecular design of novel photodegradation agents of amyloid fibrils and also expand the biomedical application of porphyrin for photosensitization.

UR - http://www.scopus.com/inward/record.url?scp=85086182309&partnerID=8YFLogxK

U2 - 10.1039/c9nj06082k

DO - 10.1039/c9nj06082k

M3 - Journal article

AN - SCOPUS:85086182309

VL - 44

SP - 9438

EP - 9443

JO - New Journal of Chemistry

JF - New Journal of Chemistry

SN - 1144-0546

IS - 22

ER -