scholarly journals Prebiotic amino acids bind to and stabilize prebiotic fatty acid membranes

2019 ◽  
Vol 116 (35) ◽  
pp. 17239-17244 ◽  
Author(s):  
Caitlin E. Cornell ◽  
Roy A. Black ◽  
Mengjun Xue ◽  
Helen E. Litz ◽  
Andrew Ramsay ◽  
...  

The membranes of the first protocells on the early Earth were likely self-assembled from fatty acids. A major challenge in understanding how protocells could have arisen and withstood changes in their environment is that fatty acid membranes are unstable in solutions containing high concentrations of salt (such as would have been prevalent in early oceans) or divalent cations (which would have been required for RNA catalysis). To test whether the inclusion of amino acids addresses this problem, we coupled direct techniques of cryoelectron microscopy and fluorescence microscopy with techniques of NMR spectroscopy, centrifuge filtration assays, and turbidity measurements. We find that a set of unmodified, prebiotic amino acids binds to prebiotic fatty acid membranes and that a subset stabilizes membranes in the presence of salt and Mg2+. Furthermore, we find that final concentrations of the amino acids need not be high to cause these effects; membrane stabilization persists after dilution as would have occurred during the rehydration of dried or partially dried pools. In addition to providing a means to stabilize protocell membranes, our results address the challenge of explaining how proteins could have become colocalized with membranes. Amino acids are the building blocks of proteins, and our results are consistent with a positive feedback loop in which amino acids bound to self-assembled fatty acid membranes, resulting in membrane stabilization and leading to more binding in turn. High local concentrations of molecular building blocks at the surface of fatty acid membranes may have aided the eventual formation of proteins.

RSC Advances ◽  
2015 ◽  
Vol 5 (108) ◽  
pp. 89025-89029 ◽  
Author(s):  
Vandana Singh ◽  
Mohan Monisha ◽  
Roy Anindya ◽  
Prolay Das

DNA–organic hybrid molecular building blocks are generated by covalent conjugation of the carboxyl groups of protoporphyrin IX with the amine functional groups of modified DNA oligomers.


2014 ◽  
Vol 1663 ◽  
Author(s):  
Garima Thakur ◽  
Kovur Prashanthi ◽  
Thomas Thundat

ABSTRACTSelf–assembly of molecular building blocks provides an interesting route to produce well-defined chemical structures. Tailoring the functionalities on the building blocks and controlling the time of self-assembly could control the properties as well as the structure of the resultant patterns. Spontaneous self-assembly of biomolecules can generate bio-interfaces for myriad of potential applications. Here we report self-assembled patterning of human serum albumin (HSA) protein in to ring structures on a polyethylene glycol (PEG) modified gold surface. The structure of the self-assembled protein molecules and kinetics of structure formation entirely revolved around controlling the nucleation of the base layer. The formation of different sizes of ring patterns is attributed to growth conditions of the PEG islands for bio-conjugation. These assemblies might be beneficial in forming structurally ordered architectures of active proteins such as HSA or other globular proteins.


Author(s):  
Jianxun Shen ◽  
Pauline M. Schwartz ◽  
Carl Barratt

On the primitive Earth, both L- and D-amino acids would have been present. However, only L-amino acids are essential blocks to construct proteins in modern life. To study the relative stability of homochiral and heterochiral peptides, a variety of computational methods were employed. 10 prebiotic amino acids (Gly, Ala, Asp, Glu, Ile, Leu, Pro, Ser, Thr, and Val) were previously determined by multiple previous meteorite, spark discharge, and hydrothermal vent studies. We focused on what had been reported as primary early Earth polypeptide analogs: 1ARK, 1PPT, 1ZFI, and 2LZE. Tripeptide composed of only Asp, Ser, and Val exemplified that different positions (i.e., N-terminus, C-terminus, and middle) made a difference in minimal folding energy of peptides, while the classification of amino acid (hydrophobic, acidic, or hydroxylic) did not show significant difference. Hierarchical cluster analysis for dipeptides with all possible combinations of the proposed 10 prebiotic amino acids and their D-amino acid substituted derivatives generated five clusters. Prebiotic polypeptides were built up to test the significance of molecular fluctuations, secondary structure occupancies, and folding energy differences based on these clusters. Most interestingly, among 129 residues, mutation sensitivity profiles presented that the ratio of more stable to less stable to equally stable D-amino acids was about 1:1:1. In conclusion, some combinations of a mixture of L- and D-amino acids can act as essential building blocks of life. Peptides with α-helices, long β-sheets, and long loops are usually less sensitive to D-amino acid replacements in comparison to short β-sheets.


Author(s):  
Graham Patrick

From very simple molecular building blocks, life has created an astonishing diversity of molecules, some of which are extremely complex structures that prove very difficult to synthesize in a laboratory. ‘The chemistry of life’ describes how proteins, which serve a myriad of purposes, and nucleic acids, another form of biopolymer, are constructed from molecular building blocks called amino acids and nucleotides respectively. It goes on to explain the polymerization processes involved in the biosynthesis of many other natural products; the functions of proteins, DNA, and RNA; and the different theories proposed to explain chemical evolution, or prebiotic chemistry. Enzymes and nucleic acids are increasingly being used in commercial applications.


2021 ◽  
Vol 12 (4) ◽  
pp. 5131-5149

Proper protein production is a serious challenge for the future. Insects represent an innovative food source and are extremely nutritious, as they have a high content of proteins and a well-balanced nutrient profile. This study focuses on the positive reasons for the use of insects as a food source and examines the contribution of insects to the human diet and the growing demand for cheap proteins in the food industry. In addition, in the present study, analyzes were performed to determine the nutritional value of mealworms and commercially available cricket flour. Moisture, ash, Total Energy Value, proteins, amino acids, fat, fatty acid profiles, carbohydrates, dietary fiber, and minerals were identified. According to the results, the samples have a high protein content and high concentrations of various amino acids (especially the essential amino acids). They also have a well-balanced fatty acid profile, high in polyunsaturated, monounsaturated fatty acids and many minerals. The main tasks are the dissemination of knowledge, the change of the process for obtaining edible insects, the development of the edible insect food industry, the expansion of the composition of already used insects, and the future conduct of research on risks to human health.


2017 ◽  
Vol 73 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Sergey G. Arkhipov ◽  
Evgeniy A. Losev ◽  
Elena V. Boldyreva

Molecular salts and cocrystals of amino acids have potential applications as molecular materials with nonlinear optical, ferroelectric, piezoelectric, and other various target physical properties. The wide choice of amino acids and coformers makes it possible to design various crystal structures. The amino acid–maleic acid system provides a perfect example of a rich variety of crystal structures with different stoichiometries, symmetries and packing motifs built from the molecular building blocks, which are either exactly the same, or differ merely by protonation or as optical isomers. The present paper reports the crystal structures of two new salts of the DL-norvaline–maleic acid system with 1:1 and 2:1 stoichiometries, namely DL-norvalinium hydrogen maleate, C5H12NO2 +·C4H3O4 −, (I), and DL-norvalinium hydrogen maleate–DL-norvaline, C5H12NO2 +·C4H3O4 −·C5H11NO2, (II). These are the first examples of molecular salts of DL-norvaline with an organic anion. The crystal structure of (I) has the same C 2 2(12) structure-forming motif which is common for hydrogen maleates of amino acids. The structure of (II) has dimeric cations. Of special interest is that the single crystals of (I) which are originally formed on crystallization from aqueous solution transform into single crystals of (II) if stored in the mother liquor for several hours.


2021 ◽  
Author(s):  
Qiuke Li ◽  
Jinze Li ◽  
Weikang Yu ◽  
Zhihua Wang ◽  
Jiawei Li ◽  
...  

Abstract BackgroundAcid-tolerant enteric pathogens could evade small intestinal acid barriers, colonizing and infecting the intestinal tract. Whereas broad-spectrum antibiotics are not the best therapeutic strategy because of the disruption of intestinal flora caused by its indiscriminate antimicrobial activity against beneficial and harmful bacteria. So that is what inspired us to combine pH regulation with nanotechnology to develop a pH-triggered site-targeted antimicrobial peptide with entrapping function. ResultsAccording to the features of amino-acid building blocks and the diagonal cation–π interaction principle, a self-assembled peptide (SAP) was designed, and the results showed that changes in pH conditions could trigger the transformation of the microstructure of the nanopeptide, which has great antimicrobial activity against Escherichia coli, Salmonella typhimurium, Listeria monocytogenes, and Bacillus cereus under acidic conditions by disrupting bacterial membrane integrity, and great biocompatibility in vivo and in vitro and high tolerance. Moreover, SAP at high concentrations showed the entrapment property, which plays an important role in phagocytic clearance in the infection forces.ConclusionsOur study revealed the antibacterial activity of a short β-hairpin forming self-assembled peptide and establishes an innovative design strategy for peptide-based nanomaterials and a new treatment strategy for gastrointestinal bacterial infection.


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