Collagen Structured Hydration
Collagen is a triple-helical protein unique to the extracellular matrix, conferring rigidity and stability to tissues such as bone and tendon. For the [(PPG)10]3 collagen-mimetic peptide at room temperature, our molecular dynamics simulations show that these properties result in a remarkably ordered first hydration layer of water molecules hydrogen bonded to the backbone carbonyl (bb-CO) oxygen atoms. This originates from the following observations. The radius of gyration attests that the PPG triplets are organized along a straight line, so that all triplets (excepting the ends) are equivalent. The solvent-accessible surface area (SASA) for the bb-CO oxygens shows a repetitive regularity for every triplet. This leads to water occupancy of the bb-CO sites following a similar regularity. In the crystal-phase X-ray data, as well as in our 100 K simulations, we observe a 0-2-1 water occupancy in the P-P-G triplet. Surprisingly, a similar (0-1.7-1) regularity is maintained in the liquid phase, in spite of the sub-nsec water exchange rates, because the bb-CO sites rarely remain vacant. The manifested ordered first-shell water molecules are expected to produce a cylindrical electrostatic potential around the peptide, to be investigated in future work.
Medienart: |
E-Artikel |
---|
Erscheinungsjahr: |
2023 |
---|---|
Erschienen: |
2023 |
Enthalten in: |
Zur Gesamtaufnahme - volume:13 |
---|---|
Enthalten in: |
Biomolecules - 13(2023), 12 vom: 04. Dez. |
Sprache: |
Englisch |
---|
Beteiligte Personen: |
Biswal, Satyaranjan [VerfasserIn] |
---|
Links: |
---|
Themen: |
059QF0KO0R |
---|
Anmerkungen: |
Date Completed 25.12.2023 Date Revised 04.01.2024 published: Electronic Citation Status MEDLINE |
---|
doi: |
10.3390/biom13121744 |
---|
funding: |
|
---|---|
Förderinstitution / Projekttitel: |
|
PPN (Katalog-ID): |
NLM366272810 |
---|
LEADER | 01000caa a22002652 4500 | ||
---|---|---|---|
001 | NLM366272810 | ||
003 | DE-627 | ||
005 | 20240108141746.0 | ||
007 | cr uuu---uuuuu | ||
008 | 231227s2023 xx |||||o 00| ||eng c | ||
024 | 7 | |a 10.3390/biom13121744 |2 doi | |
028 | 5 | 2 | |a pubmed24n1248.xml |
035 | |a (DE-627)NLM366272810 | ||
035 | |a (NLM)38136615 | ||
035 | |a (PII)1744 | ||
040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
041 | |a eng | ||
100 | 1 | |a Biswal, Satyaranjan |e verfasserin |4 aut | |
245 | 1 | 0 | |a Collagen Structured Hydration |
264 | 1 | |c 2023 | |
336 | |a Text |b txt |2 rdacontent | ||
337 | |a ƒaComputermedien |b c |2 rdamedia | ||
338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
500 | |a Date Completed 25.12.2023 | ||
500 | |a Date Revised 04.01.2024 | ||
500 | |a published: Electronic | ||
500 | |a Citation Status MEDLINE | ||
520 | |a Collagen is a triple-helical protein unique to the extracellular matrix, conferring rigidity and stability to tissues such as bone and tendon. For the [(PPG)10]3 collagen-mimetic peptide at room temperature, our molecular dynamics simulations show that these properties result in a remarkably ordered first hydration layer of water molecules hydrogen bonded to the backbone carbonyl (bb-CO) oxygen atoms. This originates from the following observations. The radius of gyration attests that the PPG triplets are organized along a straight line, so that all triplets (excepting the ends) are equivalent. The solvent-accessible surface area (SASA) for the bb-CO oxygens shows a repetitive regularity for every triplet. This leads to water occupancy of the bb-CO sites following a similar regularity. In the crystal-phase X-ray data, as well as in our 100 K simulations, we observe a 0-2-1 water occupancy in the P-P-G triplet. Surprisingly, a similar (0-1.7-1) regularity is maintained in the liquid phase, in spite of the sub-nsec water exchange rates, because the bb-CO sites rarely remain vacant. The manifested ordered first-shell water molecules are expected to produce a cylindrical electrostatic potential around the peptide, to be investigated in future work | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
650 | 4 | |a SASA | |
650 | 4 | |a collagen | |
650 | 4 | |a hydration | |
650 | 4 | |a hydrogen bond | |
650 | 4 | |a radius of gyration | |
650 | 4 | |a residence time | |
650 | 4 | |a water | |
650 | 7 | |a Peptides |2 NLM | |
650 | 7 | |a Water |2 NLM | |
650 | 7 | |a 059QF0KO0R |2 NLM | |
650 | 7 | |a Solvents |2 NLM | |
650 | 7 | |a Collagen |2 NLM | |
650 | 7 | |a 9007-34-5 |2 NLM | |
700 | 1 | |a Agmon, Noam |e verfasserin |4 aut | |
773 | 0 | 8 | |i Enthalten in |t Biomolecules |d 2011 |g 13(2023), 12 vom: 04. Dez. |w (DE-627)NLM228347106 |x 2218-273X |7 nnns |
773 | 1 | 8 | |g volume:13 |g year:2023 |g number:12 |g day:04 |g month:12 |
856 | 4 | 0 | |u http://dx.doi.org/10.3390/biom13121744 |3 Volltext |
912 | |a GBV_USEFLAG_A | ||
912 | |a GBV_NLM | ||
951 | |a AR | ||
952 | |d 13 |j 2023 |e 12 |b 04 |c 12 |