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Akdis, C.

Publications and source records attributed to Akdis, C..

2 recordsLinked to original sources

Bioconvergence of sound-guided and supramolecular assembly strategies to create peptide-protein composite hydrogels with predictable shape-to-function features

Purely protein-based hydrogels are widely used in tissue engineering for their biomimicry and biocompatibility, yet remain challenging to tailor with precision and predictability at biological and mechanical levels. To overcome this, synthetic self-assembling peptide amphiphiles (PAs) offer opportunities for supramolecular customization, both as single-phase materials and co-assembled with proteins to create hybrid nanocomposites with emerging functionalities. Similarly, contactless, sound-guided bioassembly techniques using liquid-phase hydrogel precursors are emerging as strategic tools for obtaining structured and functional hydrogels. Leveraging these advances, here a fast, contactless, one-pot bioassembly strategy merging supramolecular PA self-assembly with sound-guided patterning to fabricate hybrid peptide-protein hydrogels with programmable shape-to-function features is presented. Using fibrin as proof-of-concept, material performance is biologically enhanced by incorporating growth factor-binding PAs, while inorganic microparticles are embedded and spatially organized via acoustic fields to tune mechanical properties. This strategy allows predictable tuning of composite stiffness and architecture by adjusting sound wave frequency, with acoustic fields guiding material organization from micro-to-macroscale. Composite hydrogels result highly permissive to cell infiltration in vitro and versatile platform to tune immune cell-material interactions. This modular biofabrication platform integrating supramolecular and sound-guided processes can be generalized to other building blocks opening unique opportunities for scalable, tunable, and hierarchically-organized biomaterials.

bioengineering↗

Regulation of mRNA transcripts, protein isoforms, glycosylation and spatial localization of ACE2 and other SARS-CoV-2-associated molecules in human airway epithelium upon viral infection and type 2 inflammation

SARS-CoV-2 infection continues to pose a significant life threat, especially in patients with comorbidities. It remains unknown, if asthma or allergen- and virus-induced airway inflammation are risk factors or can constitute some forms of protection against COVID-19. ACE2 and other SARS-CoV-2-related host proteins are limiting factors of an infection, expression of which is regulated in a more complex way than previously anticipated. Hence, we studied the expression of ACE2 mRNA and protein isoforms, together with its glycosylation and spatial localization in house dust mite (HDM)-, interleukin-13 (IL-13)- and human rhinovirus (RV)-induced inflammation in the primary human bronchial airway epithelium of healthy subjects and patients with asthma. IL-13 decreased the expression of long ACE2 mRNA and glycosylation of full-length ACE2 protein via alteration of the N-linked glycosylation process, limiting its availability on the apical side of ciliated cells. RV infection increased short ACE2 mRNA, but it did not influence its protein expression. HDM exposure did not affect ACE2 mRNA or protein. IL-13 and RV significantly regulated mRNA, but not protein expression of TMPRSS2 and NRP1. Regulation of ACE2 and other host proteins was similar in healthy and asthmatic epithelium, underlining the lack of intrinsic differences, but rather the dependence on the inflammatory milieu in the airways.

immunology↗