Self‐assembling amyloid‐like peptides as exogenous second harmonic probes for bioimaging applications

Ni, Ming; Zhuo, Shuangmu; Iliescu, Ciprian; So, Peter T. C.; Yu, Hanry; Hauser, Charlotte

doi:10.1002/jbio.201900065

Cited by 21 publications

(16 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Alpha-helical conformations have also been associated to amyloid fibril formation. Certain peptides and proteins that present well defined α-helical structures undergo conformational changes into β-pleated structures that in turn aggregate into amyloid fibrils [103][104][105][106][107], while other peptides or proteins maintain its α-helical conformation during the aggregation cascade, forming "cross-α" structures. Cross-α structures are also formed by elongated unbranched fibrils, and display the ability to bind thioflavin-T with the characteristic enhanced fluorescence emission.…”

Section: The Cross-α Amyloid-like Fibrilmentioning

confidence: 99%

Structure and Aggregation Mechanisms in Amyloids

2020

View full text Add to dashboard Cite

The aggregation of a polypeptide chain into amyloid fibrils and their accumulation and deposition into insoluble plaques and intracellular inclusions is the hallmark of several misfolding diseases known as amyloidoses. Alzheimer′s, Parkinson′s and Huntington’s diseases are some of the approximately 50 amyloid diseases described to date. The identification and characterization of the molecular species critical for amyloid formation and disease development have been the focus of intense scrutiny. Methods such as X-ray and electron diffraction, solid-state nuclear magnetic resonance spectroscopy (ssNMR) and cryo-electron microscopy (cryo-EM) have been extensively used and they have contributed to shed a new light onto the structure of amyloid, revealing a multiplicity of polymorphic structures that generally fit the cross-β amyloid motif. The development of rational therapeutic approaches against these debilitating and increasingly frequent misfolding diseases requires a thorough understanding of the molecular mechanisms underlying the amyloid cascade. Here, we review the current knowledge on amyloid fibril formation for several proteins and peptides from a kinetic and thermodynamic point of view, the structure of the molecular species involved in the amyloidogenic process, and the origin of their cytotoxicity.

show abstract

Section: The Cross-α Amyloid-like Fibrilmentioning

confidence: 99%

Structure and Aggregation Mechanisms in Amyloids

2020

View full text Add to dashboard Cite

show abstract

“…A distinct difference in the organization of collagen fibers between normal and diseased corneas could be observed using SHG, which suggests that it can be used as a minimal-invasive diagnostic tool. Thus, this feature would make this class of amyloid-like peptides useful tools for label-free bioimaging techniques and diagnostic purposes [221].…”

Section: Amyloid In Bioimaging: Bioorganic Nanodotsmentioning

confidence: 99%

“What Doesn’t Kill You Makes You Stronger”: Future Applications of Amyloid Aggregates in Biomedicine

et al. 2020

Self Cite

View full text Add to dashboard Cite

Amyloid proteins are linked to the pathogenesis of several diseases including Alzheimer’s disease, but at the same time a range of functional amyloids are physiologically important in humans. Although the disease pathogenies have been associated with protein aggregation, the mechanisms and factors that lead to protein aggregation are not completely understood. Paradoxically, unique characteristics of amyloids provide new opportunities for engineering innovative materials with biomedical applications. In this review, we discuss not only outstanding advances in biomedical applications of amyloid peptides, but also the mechanism of amyloid aggregation, factors affecting the process, and core sequences driving the aggregation. We aim with this review to provide a useful manual for those who engineer amyloids for innovative medicine solutions.

show abstract

“…With the peptide bonds identified as SHG harmophores, it seems plausible to engineer genetically-encoded SHG probes. Synthetic peptides have been designed as SHG probes for studying various dynamics such as membrane penetration (Rao et al, 2014) and amyloidosis (Ni et al, 2019). Interestingly, the cyclic tripeptide chromophore of GFP, which exhibits an unusually large intramolecular charge transfer (de Meulenaere et al, 2009), has been recognized as a source of SHG (Lewis et al, 1999; Khatchatouriants et al, 2000; Asselberghs et al, 2008).…”

Section: Exogenous Molecules For Functional Shg Imagingmentioning

confidence: 99%

Harmonic Generation Microscopy 2.0: New Tricks Empowering Intravital Imaging for Neuroscience

Lim

2019

Front. Mol. Biosci.

View full text Add to dashboard Cite

Optical harmonic generation, e.g., second- (SHG) and third-harmonic generation (THG), provides intrinsic contrasts for three-dimensional intravital microscopy. Contrary to two-photon excited fluorescence (TPEF), however, they have found relatively specialized applications, such as imaging collagenous and non-specific tissues, respectively. Here we review recent advances that broaden the capacity of SHG and THG for imaging the central nervous system in particular. The fundamental contrast mechanisms are reviewed as they encode novel information including molecular origin, spectroscopy, functional probes, and image analysis, which lay foundations for promising future applications in neuroscience.

show abstract

Self‐assembling amyloid‐like peptides as exogenous second harmonic probes for bioimaging applications

Cited by 21 publications

References 39 publications

Structure and Aggregation Mechanisms in Amyloids

Structure and Aggregation Mechanisms in Amyloids

“What Doesn’t Kill You Makes You Stronger”: Future Applications of Amyloid Aggregates in Biomedicine

Harmonic Generation Microscopy 2.0: New Tricks Empowering Intravital Imaging for Neuroscience

Contact Info

Product

Resources

About