TY - JOUR
T1 - The Role of Concentration on Drop Formation and Breakup of Collagen, Fibrinogen, and Thrombin Solutions during Inkjet Bioprinting
AU - Gudapati, Hemanth
AU - Ozbolat, Ibrahim T.
N1 - Funding Information:
The authors are grateful for the valuable insights provided by Dr. Ralph H. Colby from the Department of Materials Science and Engineering at Penn State on the behavior of protein molecules in an extensional flow and at the liquid/air and liquid/solid interfaces. The authors are grateful for the feedback from Dr. Bruce Gluckman from the Engineering Science and Mechanics Department at Penn State. This research has been supported by the Osteology Foundation Award #15-042, National Institute of Dental and Craniofacial Research Award R01DE028614, and the Hartz Career Development Professorship (I.T.O.).
Publisher Copyright:
©
PY - 2020/12/22
Y1 - 2020/12/22
N2 - The influence of protein concentration on drop formation and breakup of aqueous solutions of fibrous proteins collagen and fibrinogen and globular protein thrombin in different concentration regimes has been investigated during drop-on-demand (DOD) inkjet printing. The capillary-driven thinning and breakup of dilute collagen, fibrinogen, and thrombin solutions, the solutions in which protein molecules are far away from each other, are predominantly resisted by inertial force. Although the capillary-driven thinning and breakup of semidilute unentangled collagen and fibrinogen solutions, the solutions in which protein molecules begin to interpenetrate each other, are predominantly resisted by inertial force on the initial onset of necking, the breakup of droplets is delayed because of the resistance of elastic force. The resistance of viscous force to the necking and breakup of both the dilute and semidilute unentangled protein solutions is negligible. Aggregates or subvisible particles (between 1 and 100 μm) constantly disrupt the formation of droplets for the semidilute unentangled protein solutions, even when their inverse Ohnesorge number (Z) is within the printability range of 4 ≤ Z ≤ 14. Although aggregates are present in the dilute protein solutions, they do not disrupt the formation of droplets.
AB - The influence of protein concentration on drop formation and breakup of aqueous solutions of fibrous proteins collagen and fibrinogen and globular protein thrombin in different concentration regimes has been investigated during drop-on-demand (DOD) inkjet printing. The capillary-driven thinning and breakup of dilute collagen, fibrinogen, and thrombin solutions, the solutions in which protein molecules are far away from each other, are predominantly resisted by inertial force. Although the capillary-driven thinning and breakup of semidilute unentangled collagen and fibrinogen solutions, the solutions in which protein molecules begin to interpenetrate each other, are predominantly resisted by inertial force on the initial onset of necking, the breakup of droplets is delayed because of the resistance of elastic force. The resistance of viscous force to the necking and breakup of both the dilute and semidilute unentangled protein solutions is negligible. Aggregates or subvisible particles (between 1 and 100 μm) constantly disrupt the formation of droplets for the semidilute unentangled protein solutions, even when their inverse Ohnesorge number (Z) is within the printability range of 4 ≤ Z ≤ 14. Although aggregates are present in the dilute protein solutions, they do not disrupt the formation of droplets.
UR - http://www.scopus.com/inward/record.url?scp=85097814614&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85097814614&partnerID=8YFLogxK
U2 - 10.1021/acs.langmuir.0c02926
DO - 10.1021/acs.langmuir.0c02926
M3 - Article
C2 - 33295180
AN - SCOPUS:85097814614
SN - 0743-7463
VL - 36
SP - 15373
EP - 15385
JO - Langmuir
JF - Langmuir
IS - 50
ER -