scholarly journals Peptide-Based Supramolecular Systems Chemistry

2021 ◽  
Author(s):  
Fahmeed Sheehan ◽  
Deborah Sementa ◽  
Ankit Jain ◽  
Mohit Kumar ◽  
Mona Tayarani-Najjaran ◽  
...  
Life ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 49 ◽  
Author(s):  
Augustin Lopez ◽  
Michele Fiore

Protocells are supramolecular systems commonly used for numerous applications, such as the formation of self-evolvable systems, in systems chemistry and synthetic biology. Certain types of protocells imitate plausible prebiotic compartments, such as giant vesicles, that are formed with the hydration of thin films of amphiphiles. These constructs can be studied to address the emergence of life from a non-living chemical network. They are useful tools since they offer the possibility to understand the mechanisms underlying any living cellular system: Its formation, its metabolism, its replication and its evolution. Protocells allow the investigation of the synergies occurring in a web of chemical compounds. This cooperation can explain the transition between chemical (inanimate) and biological systems (living) due to the discoveries of emerging properties. The aim of this review is to provide an overview of relevant concept in prebiotic protocell research.


2015 ◽  
Vol 10 (2) ◽  
pp. 111-119 ◽  
Author(s):  
Elio Mattia ◽  
Sijbren Otto

2017 ◽  
Vol 46 (9) ◽  
pp. 2543-2554 ◽  
Author(s):  
Gonen Ashkenasy ◽  
Thomas M. Hermans ◽  
Sijbren Otto ◽  
Annette F. Taylor

A series of exciting phenomena that can occur in supramolecular systems away from equilibrium are reviewed.


2019 ◽  
Vol 3 (5) ◽  
pp. 435-443 ◽  
Author(s):  
Addy Pross

Despite the considerable advances in molecular biology over the past several decades, the nature of the physical–chemical process by which inanimate matter become transformed into simplest life remains elusive. In this review, we describe recent advances in a relatively new area of chemistry, systems chemistry, which attempts to uncover the physical–chemical principles underlying that remarkable transformation. A significant development has been the discovery that within the space of chemical potentiality there exists a largely unexplored kinetic domain which could be termed dynamic kinetic chemistry. Our analysis suggests that all biological systems and associated sub-systems belong to this distinct domain, thereby facilitating the placement of biological systems within a coherent physical/chemical framework. That discovery offers new insights into the origin of life process, as well as opening the door toward the preparation of active materials able to self-heal, adapt to environmental changes, even communicate, mimicking what transpires routinely in the biological world. The road to simplest proto-life appears to be opening up.


2011 ◽  
Author(s):  
Chad A. Mirkin ◽  
Joseph T. Hupp

2020 ◽  
Vol 61 (5) ◽  
pp. 786-793
Author(s):  
N. V. Potapova ◽  
O. T. Kasaikina ◽  
M. P. Berezin ◽  
I. G. Plashchina

Biomolecules ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 501
Author(s):  
Ptak-Kaczor Magdalena ◽  
Kwiecińska Klaudia ◽  
Korchowiec Jacek ◽  
Chłopaś Katarzyna ◽  
Banach Mateusz ◽  
...  

In the search for new carriers capable of transporting toxic drugs to a target, particular attention has been devoted to supramolecular systems with a ribbon-like micellar structure of which Congo red is an example. A special promise of the possible use of such systems for directing drugs to a target emerges from their particular affinity to immune complexes and as an independent property, binding many organic compounds including drugs by intercalation. Serum albumin also appeared able to bind micellar particles of such systems. It may protect them against dilution in transport. The mathematical tool, which relies on analysis of the distribution of polarity and hydrophobicity in protein molecules (fuzzy oil drop model), has been used to find the location of binding area in albumin as well as anchorage site for Congo red in heated IgG light chain used as a model presenting immunoglobulin-like structures. Results confirm the suggested formerly binding site of Congo red in V domain of IgG light chain and indicated the cleft between pseudo-symmetric domains of albumin as the area of attachment for the dye.


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