Structure and mechanism behind the inhibitory effect of water soluble metalloporphyrins on Aβ<sub>1–42</sub>aggregation

Zhang, Qianqian; Liu, Yiqing; Wu, Jinming; Zeng, Lingfang; Wei, Jingjing; Fu, Shitao; Ye, Huixian; Li, Yong; Gao, Zhonghong

doi:10.1039/d1qi01434j

Inorg. Chem. Front.

2022

DOI: 10.1039/d1qi01434j

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Structure and mechanism behind the inhibitory effect of water soluble metalloporphyrins on Aβ_1–42aggregation

Qianqian Zhang

Yiqing Liu

Jinming Wu

et al.

Abstract: Although the exact molecular mechanism of the pathogenesis of Alzheimer’s disease (AD) is still unclear, compounds that can inhibit the aggregation of amyloid-β peptide (Aβ1-42) or scavenge the highly toxic...

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Cited by 8 publications

References 69 publications

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A Spectroscopic Study on the Amyloid‐β Interaction with Clicked Peptide‐Porphyrin Conjugates: a Vision Toward the Detection of Aβ Peptides in Aqueous Solution

Tosto,

Zimbone,

Sabatino

et al. 2024

ChemBioChem

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Alzheimer’s disease (AD) is a multifactorial form of dementia mainly affecting people in the elderly, but no effective cure is available. According to the amyloid hypothesis the aggregation of Amyloid‐β (Aβ) into oligomeric toxic species is believed to concur with the onset and progression of the disease heavily. By using a click chemistry approach, we conjugated a suitable designed peptide sequence to a metalloporphyrin moiety to obtain three hybrid peptide systems to be studied for their interact ion with Amyloid‐β peptides. The aim is to get new tools for the diagnosis and therapy in AD. The results described in this study, which were obtained through spectroscopic techniques (UV‐Vis, CD, Bis‐Ans and intrinsic porphyrin Fluorescence), Microfluidics (GCI) and cell biology (MTT, Live cell imaging and flow cytometry), reveal interesting features about the structure‐activity relationships connecting these conjugates with the interaction with Aβ, as well as on their potential use as sensing systems. In our opinion the data reported in this paper make the porphyrin‐peptide conjugates highly compelling for further exploration as spectroscopic probes to detect Aβ biomarkers in biological fluids.

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A Spectroscopic Study on the Amyloid‐β Interaction with Clicked Peptide‐Porphyrin Conjugates: a Vision Toward the Detection of Aβ Peptides in Aqueous Solution

Tosto,

Zimbone,

Sabatino

et al. 2024

ChemBioChem

View full text Add to dashboard Cite

show abstract

Approaches for developing peptide- and metal complexes- or chelators-based leads for anti-amyloid drugs

Florio,

Marasco,

Manna

2025

Inorganica Chimica Acta

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Inhibitory activities of flavonoids from Scutellaria baicalensis Georgi on amyloid aggregation related to type 2 diabetes and the possible structural requirements for polyphenol in inhibiting the nucleation phase of hIAPP aggregation

Wang

Wei

et al. 2022

International Journal of Biological Macromolecules

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Structure and mechanism behind the inhibitory effect of water soluble metalloporphyrins on Aβ_1–42aggregation

Abstract: Although the exact molecular mechanism of the pathogenesis of Alzheimer’s disease (AD) is still unclear, compounds that can inhibit the aggregation of amyloid-β peptide (Aβ1-42) or scavenge the highly toxic...

Cited by 8 publications

References 69 publications

A Spectroscopic Study on the Amyloid‐β Interaction with Clicked Peptide‐Porphyrin Conjugates: a Vision Toward the Detection of Aβ Peptides in Aqueous Solution

A Spectroscopic Study on the Amyloid‐β Interaction with Clicked Peptide‐Porphyrin Conjugates: a Vision Toward the Detection of Aβ Peptides in Aqueous Solution

Approaches for developing peptide- and metal complexes- or chelators-based leads for anti-amyloid drugs

Inhibitory activities of flavonoids from Scutellaria baicalensis Georgi on amyloid aggregation related to type 2 diabetes and the possible structural requirements for polyphenol in inhibiting the nucleation phase of hIAPP aggregation

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Structure and mechanism behind the inhibitory effect of water soluble metalloporphyrins on Aβ1–42aggregation

Abstract: Although the exact molecular mechanism of the pathogenesis of Alzheimer’s disease (AD) is still unclear, compounds that can inhibit the aggregation of amyloid-β peptide (Aβ1-42) or scavenge the highly toxic...

Cited by 8 publications

References 69 publications

A Spectroscopic Study on the Amyloid‐β Interaction with Clicked Peptide‐Porphyrin Conjugates: a Vision Toward the Detection of Aβ Peptides in Aqueous Solution

A Spectroscopic Study on the Amyloid‐β Interaction with Clicked Peptide‐Porphyrin Conjugates: a Vision Toward the Detection of Aβ Peptides in Aqueous Solution

Approaches for developing peptide- and metal complexes- or chelators-based leads for anti-amyloid drugs

Inhibitory activities of flavonoids from Scutellaria baicalensis Georgi on amyloid aggregation related to type 2 diabetes and the possible structural requirements for polyphenol in inhibiting the nucleation phase of hIAPP aggregation

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Product

Resources

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Structure and mechanism behind the inhibitory effect of water soluble metalloporphyrins on Aβ_1–42aggregation