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Related Concept Videos

ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
Mechanical Protein Functions01:58

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 

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Fabrication of Carbon-Based Ionic Electromechanically Active Soft Actuators
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Protein Biomaterials with Muscle-like Water-Driven Actuation.

Sanam Bista1, Ionel Popa1

  • 1Department of Physics and Astronomy, University of Wisconsin-Milwaukee, 3135 N. Maryland Ave, Milwaukee, Wisconsin 53211, United States.

ACS Applied Materials & Interfaces
|January 3, 2026
PubMed
Summary
This summary is machine-generated.

Researchers developed novel protein-based actuators from bovine serum albumin (BSA) hydrogels that mimic muscle contraction. These biomaterials exhibit fast, reversible shape changes and motion, driven by ethanol and water interactions.

Keywords:
Marangoni flowamyloid fibrilshydrogel actuatorsprogrammable biomaterialsprotein-based biomaterialsshape-memorysolvent-exchange motorsolvent-responsive actuation

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Area of Science:

  • Biomaterials Science
  • Protein Engineering
  • Soft Robotics

Background:

  • Man-made shape-morphing biomaterials typically exhibit slow actuation compared to biological muscles.
  • Developing artificial actuators with muscle-like speed and reversibility remains a significant challenge in biomaterials science.

Purpose of the Study:

  • To engineer a novel class of protein-based actuators capable of rapid, reversible shape changes and motion.
  • To mimic muscle contraction mechanisms using protein hydrogels.
  • To explore applications in smart biomaterials and microactuators.

Main Methods:

  • Utilized bovine serum albumin (BSA) hydrogels to create protein-based actuators.
  • Induce fibril formation using varying ethanol concentrations (40-99%) to control shape changes.
  • Investigated water-driven motion, including pulsating and rotational movement, triggered by ethanol retention.

Main Results:

  • Achieved reversible shape changes in BSA hydrogels through ethanol-induced fibril formation and aggregation.
  • Demonstrated fast, water-driven motion, including stochastic pulsations and rotational speeds up to 471 deg·s-1 in a protein-based propeller motor.
  • Showcased programmable shape changes occurring over minutes to hours, with shape recovery upon rehydration.

Conclusions:

  • Developed a novel class of protein-based actuators with muscle-like actuation speeds and reversibility.
  • The BSA hydrogel system offers a promising platform for creating advanced biomaterials with dynamic shape-morphing capabilities.
  • Potential applications include bioresponsive systems, microactuators, and soft robotics.