Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin–Myosin Interaction
Abstract
:1. Introduction
2. Results
2.1. Mechanics and Energetics of Skeletal Muscle
2.2. Fitting the Performance of Muscle Contraction with a Simple Three-State Model
2.3. Mechanics and Energetics of the Sarcomere-like Nanomachine
3. Discussion
4. Material and Methods
4.1. Experimental Data
4.2. Model Simulation
5. Conclusions
Supplementary Materials
Author Contributions
Funding
Data Availability Statement
Conflicts of Interest
References
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T0 | 1/3 T0 | |
---|---|---|
E′ (mW g−1) | 11.2 | 45.0 |
P (mW g−1) | 0 | 22.0 (Pmax) |
ATPase rate (μmol s−1 g−1) | 0.23 | 0.90 |
φ (s−1) | 1.1 | 4.3 |
E′0 (mW g−1) | E′Pmax (mW g−1) | Pmax (mW g−1) | ε, η | φ0 (s−1) | φPmax (s−1) | φPmax/φ0 | ||
---|---|---|---|---|---|---|---|---|
Mouse EDL, intact [26] | 21 °C | 134 | 214 | 57.2 | 0.28 | 12.4 | 19.8 | 1.6 |
Mouse EDL, intact [27] | 25 °C | 144 | 269 | 70 | 0.26 | 13.3 | 25 | 1.87 |
Rat IIB, skinned [28] | 12 °C | 15 | 40.2 | 9.59 | 0.24 | 1.39 | 3.7 | 2.7 |
Rabbit psoas, skinned [29] | 15 °C | 2.1 | 6 | 2.8 | ||||
Rabbit psoas, skinned [30] | 10 °C | 11.4 | 30 | (10) | 0.33 | 1.05 | 2.77 | 2.6 |
Human IIA, skinned [31] | 20 °C | 48 | 96 | 30 | 0.31 | 4.4 | 8.89 | 2 |
N = 294 | F0 (pN) | r0 | φ0 (s−1) | a/F0 | V0 (µm s−1) | Pmax (aW) | φPmax (s−1) |
---|---|---|---|---|---|---|---|
Model 1 | 433 ± 5 | 0.32 | 11.65 | 0.36 | 8.61 ± 0.16 | 462 | 35.5 |
Model 2 | 418 ± 6 | 0.31 | 11.71 | 0.22 | 6.02 ± 0.12 | 220 | 31.9 |
Model 3 | 445 ± 9 | 0.33 | 11.41 | 0.39 | 8.79 ± 0.14 | 474 | 67.2 |
N = 294 | F0 (pN) | r0 | φ0 (s−1) | a/F0 | V0 (µm s−1) | Pmax (aW) | φPmax (s−1) |
---|---|---|---|---|---|---|---|
Model 1 | 336 ± 12 | 0.24 | 2.30 | 0.34 | 2.60 ± 0.07 | 98.5 | 8.63 |
Model 2 | 291 ± 23 | 0.23 | 2.10 | 0.14 | 2.25 ± 0.03 | 45.0 | 8.45 |
Model 3 | 342 ± 21 | 0.24 | 2.40 | 0.30 | 2.67 ± 0.11 | 96.0 | 23.1 |
F0 (pN) | r0 | φ0 (s−1) | a/F0 | V0 (µm s−1) | Pmax (aW) | φPmax (s−1) | |
---|---|---|---|---|---|---|---|
N = 294 Compliance 0.01 nm pN−1 | 433 ± 5 | 0.32 | 11.65 | 0.36 | 8.61 ± 0.16 | 462 | 35.50 |
N = 16 Compliance 3.7 nm pN−1 + random | 15.8 ± 0.4 | 0.40 | 18.21 | 0.24 | 3.45 ± 0.13 | 5.45 | 26.21 |
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Pertici, I.; Bongini, L.; Caremani, M.; Reconditi, M.; Linari, M.; Piazzesi, G.; Lombardi, V.; Bianco, P. Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin–Myosin Interaction. Int. J. Mol. Sci. 2023, 24, 12324. https://doi.org/10.3390/ijms241512324
Pertici I, Bongini L, Caremani M, Reconditi M, Linari M, Piazzesi G, Lombardi V, Bianco P. Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin–Myosin Interaction. International Journal of Molecular Sciences. 2023; 24(15):12324. https://doi.org/10.3390/ijms241512324
Chicago/Turabian StylePertici, Irene, Lorenzo Bongini, Marco Caremani, Massimo Reconditi, Marco Linari, Gabriella Piazzesi, Vincenzo Lombardi, and Pasquale Bianco. 2023. "Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin–Myosin Interaction" International Journal of Molecular Sciences 24, no. 15: 12324. https://doi.org/10.3390/ijms241512324