Protein antibiotics: mind your language

Correia, Annapaula; Weimann, Aaron

doi:10.1038/s41579-020-00485-5

Cited by 6 publications

(6 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Characterization of the structure and physiochemical features of AMPs can help us to identify the novel AMPs. The new technologies, such as the new genome mining approaches using machine learning and sequence-based encodings [ 84 ] will accelerate this discovery process.…”

Section: Natural Distribution Of Ampsmentioning

confidence: 99%

Antimicrobial peptides: mechanism of action, activity and clinical potential

et al. 2021

View full text Add to dashboard Cite

The management of bacterial infections is becoming a major clinical challenge due to the rapid evolution of antibiotic resistant bacteria. As an excellent candidate to overcome antibiotic resistance, antimicrobial peptides (AMPs) that are produced from the synthetic and natural sources demonstrate a broad-spectrum antimicrobial activity with the high specificity and low toxicity. These peptides possess distinctive structures and functions by employing sophisticated mechanisms of action. This comprehensive review provides a broad overview of AMPs from the origin, structural characteristics, mechanisms of action, biological activities to clinical applications. We finally discuss the strategies to optimize and develop AMP-based treatment as the potential antimicrobial and anticancer therapeutics.

show abstract

Section: Natural Distribution Of Ampsmentioning

confidence: 99%

Antimicrobial peptides: mechanism of action, activity and clinical potential

et al. 2021

View full text Add to dashboard Cite

show abstract

“…This issue has been raised before ( Ramirez et al, 2018 ) and impedes otherwise valuable work. For instance, bioprospecting of biosynthetic gene clusters with SML-based omics data mining can yield proteins with biotechnological potential ( Correia and Weimann, 2021 ) for bioremediation, biodegradable plastic production, and sustainable biofuels ( Haque et al, 2020 ; Keasling et al, 2021 ). We therefore urge that omics data sets be uploaded in their raw form with metadata made available.…”

Section: Main Bodymentioning

confidence: 99%

Interfacing Machine Learning and Microbial Omics: A Promising Means to Address Environmental Challenges

et al. 2022

View full text Add to dashboard Cite

Microbial communities are ubiquitous and carry an exceptionally broad metabolic capability. Upon environmental perturbation, microbes are also amongst the first natural responsive elements with perturbation-specific cues and markers. These communities are thereby uniquely positioned to inform on the status of environmental conditions. The advent of microbial omics has led to an unprecedented volume of complex microbiological data sets. Importantly, these data sets are rich in biological information with potential for predictive environmental classification and forecasting. However, the patterns in this information are often hidden amongst the inherent complexity of the data. There has been a continued rise in the development and adoption of machine learning (ML) and deep learning architectures for solving research challenges of this sort. Indeed, the interface between molecular microbial ecology and artificial intelligence (AI) appears to show considerable potential for significantly advancing environmental monitoring and management practices through their application. Here, we provide a primer for ML, highlight the notion of retaining biological sample information for supervised ML, discuss workflow considerations, and review the state of the art of the exciting, yet nascent, interdisciplinary field of ML-driven microbial ecology. Current limitations in this sphere of research are also addressed to frame a forward-looking perspective toward the realization of what we anticipate will become a pivotal toolkit for addressing environmental monitoring and management challenges in the years ahead.

show abstract

“…Proteins are the molecular machines of life. 1 They carry out a hugely complex variety of biochemical functions in living cells in addition to having a huge range of technological applications, including several antibacterial formulations 2 and the new protein-based Covid-19 vaccines. 3 Under specific physicochemical conditions, the majority of proteins undergo structural transformations leading to the formation of aggregated structures known as amyloid fibrils.…”

mentioning

confidence: 99%

“…Proteins are the molecular machines of life . They carry out a hugely complex variety of biochemical functions in living cells in addition to having a huge range of technological applications, including several antibacterial formulations and the new protein-based Covid-19 vaccines . Under specific physicochemical conditions, the majority of proteins undergo structural transformations leading to the formation of aggregated structures known as amyloid fibrils. − Amyloid fibrils and, more generally, protein aggregation processes are involved in key biological mechanisms in healthy organisms − and have also been observed in several diseases, including Alzheimer’s and Parkinson’s diseases. ,,− Moreover, amyloid fibrils have been exploited as advanced materials in biomedicine, tissue engineering, renewable energy, environmental science, nanotechnology and material science. − The process that, starting from the functional folded protein monomers, leads to the formation of the mature amyloid fibrils is known as amyloidogenesis.…”

mentioning

confidence: 99%

Controlling Amyloid Fibril Properties Via Ionic Liquids: The Representative Case of Ethylammonium Nitrate and Tetramethylguanidinium Acetate on the Amyloidogenesis of Lysozyme

Pillai

Kumari

Kolagatla

et al. 2022

J. Phys. Chem. Lett.

View full text Add to dashboard Cite

Protein aggregation into amyloid fibrils has been observed in several pathological conditions and exploited in nanotechnology. It is also key in several biochemical processes. In this work, we show that ionic liquids (ILs), a vast class of organic electrolytes, can finely tune amyloid properties, opening a new landscape in basic science and applications. The representative case of ethylammonium nitrate (EAN) and tetramethyl-guanidinium acetate (TMGA) ILs on lysozyme is considered. First, atomic force microscopy has shown that the addition of EAN and TMGA leads to thicker and thinner amyloid fibrils of greater and lower electric potential, respectively, with diameters finely tunable by IL concentration. Optical tweezers and neutron scattering have shed light on their mechanism of action. TMGA interacts with the protein hydration layer only, making the relaxation dynamics of these water molecules faster. EAN interacts directly with the protein instead, making it mechanically unstable and slowing down its relaxation dynamics.

show abstract

Protein antibiotics: mind your language

Cited by 6 publications

References 4 publications

Antimicrobial peptides: mechanism of action, activity and clinical potential

Antimicrobial peptides: mechanism of action, activity and clinical potential

Interfacing Machine Learning and Microbial Omics: A Promising Means to Address Environmental Challenges

Controlling Amyloid Fibril Properties Via Ionic Liquids: The Representative Case of Ethylammonium Nitrate and Tetramethylguanidinium Acetate on the Amyloidogenesis of Lysozyme

Contact Info

Product

Resources

About