Kh Imam Zarkasyi's Life Principles In Education Of Modern Pondok Santri Darussalam Gontor In Muhammad Ridlo Zarkasyi's Book

KH Imam Zarkasyi is an ideal educator who has been successful in the development of education and teaching, especially in fostering the quality of his students. A century has passed since Pondok Modern Darussalam Gontor has continued to take part in the community. Pondok Modern Darussalam Gontor has produced alumni who already have names in the public. The motivation for success in today's society aims to remind people of success ambitions that were once forgotten for a moment. The secret of success as outlined in this article is expected to be able to stimulate thoughts and behavior to keep the spirit of fighting in the mirror from the secret of success according to KH Imam Zarkasyi. Based on this background, the problem that can be formulated is how the principle of K. H Imam Zarkasyi in educating the Darussalam Gontor Modern Islamic Boarding School students in Muhammad Ridlo Zarkasyi's book. The purpose of this study was to find out how the principle of KH Imam Zarkasyi's life in educating the students of Pondok Modern Darussalam Gontor in Muhammad Ridlo Zarkasyi's book. This type of research is library research that uses literature review material and the primary source is the book: Ajaran Kiai Gontor by Muhammad Ridlo Zarkasyi and the secondary source is taking from books, journals, articles related to research. The data analysis technique is using descriptive analysis and content analysis. The results of this study indicate that the secret of success according to KH Imam Zarkasyi in the book Ajaran Kiai Gontor by Muhammad Ridlo Zarkasyi is to get used to self-control, self-regulation and time management. Being a Muslim must be good at self-control, in the sense of jihad in all things, including fighting lust and not being wasteful in everything. Wasting time is also a waste of time. We must be able to take advantage of the time we have for a glorious future. KH Imam Zarkasyi also said "Don't get carried away with today's success". Because complacency is a disease for people who want success. From the journey of KH Imam Zarkasyi to his success, we can take the existing lessons and use them as lessons to welcome our future to achieve success as well

Chain-end modifications and sequence arrangements of antimicrobial peptoids for mediating activity and nano-assembly

Poly(N-substituted glycine) “peptoids” are an interesting class of peptidomimics that can resist proteolysis and mimic naturally found antimicrobial peptides (AMPs), which exhibit wide spectrum activity against bacteria. This work investigates the possibility of modifying peptoid AMP mimics (AMPMs) with aliphatic lipid “tails” to generate “lipopeptoids” that can assemble into micellar nanostructures, and evaluates their antimicrobial activities. Two families of AMPMs with different distributions of hydrophobic and cationic residues were employed—one with a uniform repeating amphiphilicity, the other with a surfactant-like head-to-tail amphiphilicity. To further evaluate the interplay between self-assembly and activity, the lipopeptoids were variously modified at the AMPM chain ends with a diethylene glycol (EG2) and/or a cationic group (Nlys-Nlys dipeptoid) to adjust amphiphilicity and chain flexibility. Self-assembly was investigated by critical aggregation concentration (CAC) fluorescence assays and dynamic light scattering (DLS). The structure of a key species was also verified by small-angle X-ray scattering (SAXS) and cryo-electron microscopy (cryo-EM). To screen for antibacterial properties, we measured the minimum inhibitory concentrations (MIC) against S. aureus, E. coli, and P. aeruginosa. We found that certain combinations of lipid tail and AMPM sequences exhibit increased antibacterial activity (i.e., decreased MICs). Perhaps counter-intuitively, we were particularly interested in increased MICs in combination with low CACs. Concealing antimicrobial interactions due to packing of AMPMs in nano-assemblies could pave the way to AMPMs that may be “inert” even if unintentionally released and prevent microbes from gaining resistance to the lipopeptoids. Overall, incorporation of EG2 significantly improved lipopeptoids packing while the hydrophobic tail length was found to have a major influence over the MIC. One particular sequence, which we named C15-EG2-(kss)4, exhibited a very low CAC of 34 μM (0.0075 wt.%) and a significantly increased MIC above values for the unmodified AMPM. With the sequence design trends uncovered from this study, future work will focus on discovering more species such as C15-EG2-(kss)4 and on investigating release mechanisms and the potency of the released lipopeptoids

Self-assembly of minimal peptoid sequences

Peptoids are biofunctional N-substituted glycine peptidomimics. Their self-assembly is of fundamental interest because they demonstrate alternatives to conventional peptide structures based on backbone chirality and beta-sheet hydrogen bonding. The search for self-assembling, water-soluble “minimal” sequences, be they peptide or peptidomimic, is a further challenge. Such sequences are highly desired for their compatibility with biomacromolecules and convenient synthesis for broader application. We report the self-assembly of a set of trimeric, water-soluble α-peptoids that exhibit a relatively low critical aggregation concentration (CAC ∼ 0.3 wt %). Cryo-EM and angle-resolved DLS show different sequence-dependent morphologies, namely uniform ca. 6 nm wide nanofibers, sheets, and clusters of globular assemblies. Absorbance and fluorescence spectroscopies indicate unique phenyl environments for π-interactions in the highly ordered nanofibers. Assembly of our peptoids takes place when the sequences are fully ionized, representing a departure from superficially similar amyloid-type hydrogen-bonded peptide nanostructures and expanding the horizons of assembly for sequence-specific bio- and biomimetic macromolecules

Crystallization and lamellar nanosheet formation of an aromatic dipeptoid

An aromatic peptoid analogue of the diphenylalanine dipeptide self-assembles in aqueous solution and the first crystal structure was obtained for this class of compound. This reveals molecular packing stabilized by networks of hydrogen bonds. Free-floating nanosheet lamellar structures are observed in solution, which form via cooperative intermolecular interactions driven by π stacking

Surface design for immobilization of an antimicrobial peptide mimic for efficient anti‐biofouling

Microbial surface attachment negatively impacts a wide range of devices from water purification membranes to biomedical implants. Mimics of antimicrobial peptides (AMPs) constituted from poly(N‐substituted glycine) "peptoids" are of great interest as they resist proteolysis and can inhibit a wide spectrum of microbes. We investigate how terminal modification of a peptoid AMP‐mimic and its surface immobilization affect antimicrobial activity. We also demonstrate a convenient surface modification scheme for enabling alkyne‐azide "click" coupling on amino‐functionalized surfaces. Our results verified that the N‐ and C‐terminal peptoid structures are not required for antimicrobial activity. Moreover, our peptoid immobilization density and choice of PEG tether resulted in a "volumetric" spatial separation between AMPs that, compared to past studies, enabled the highest AMP surface activity relative to bacterial attachment. Our analysis suggests the importance of spatial flexibility for membrane activity and that AMP separation may be a controlling parameter for optimizing surface anti‐biofouling

Mineralizing Coating on 3D Printed Scaffolds for the Promotion of Osseointegration

Design and fabrication of implants that can perform better than autologous bone grafts remain an unmet challenge for the hard tissue regeneration in craniomaxillofacial applications. Here, we report an integrated approach combining additive manufacturing with supramolecular chemistry to develop acellular mineralizing 3D printed scaffolds for hard tissue regeneration. Our approach relies on an elastin-like recombinamer (ELR) coating designed to trigger and guide the growth of ordered apatite on the surface of 3D printed nylon scaffolds. Three test samples including a) uncoated nylon scaffolds (referred to as “Uncoated”), b) ELR coated scaffolds (referred to as “ELR only”), and c) ELR coated and in vitro mineralized scaffolds (referred to as “Pre-mineralized”) were prepared and tested for in vitro and in vivo performance. All test samples supported normal human immortalized mesenchymal stem cell adhesion, growth, and differentiation with enhanced cell proliferation observed in the “Pre-mineralized” samples. Using a rabbit calvarial in vivo model, ‘Pre-mineralized’ scaffolds also exhibited higher bone ingrowth into scaffold pores and cavities with higher tissue-implant integration. However, the coated scaffolds (“ELR only” and “Pre-mineralized”) did not exhibit significantly more new bone formation compared to “Uncoated” scaffolds. Overall, the mineralizing coating offers an opportunity to enhance integration of 3D printed bone implants. However, there is a need to further decipher and tune their immunologic response to develop truly osteoinductive/conductive surfaces

Correction to "self-assembly of minimal peptoid sequences"

It has come to our attention that some of our cryo-electron microscopy (cryo-EM) images actually show ice contamination, (1) instead of the soft matter aggregates originally indicated in our publication. The images only relate to counterexample peptoid sequences that did not properly assemble (originally Figures 3D–K and S5E–G, I–M, and P). As such, our main finding of an ultrashort water-soluble tripeptoid assembling into ordered nanofibers is not changed. Our overall conclusions based on complementary cryo-EM, DLS, CAC, and fluorescence spectroscopy measurements are also unaffected. Nonetheless, the figures indicated and associated text require correction. In re-examining our cryo-EM data set, we found micrographs showing additional structures that are unlikely to be contaminants, which we previously took as less representative. Like the artifacts, the structures now identified are also irregular and consist of an ensemble of sizes centered around a mean. Incidentally, the mean sizes of these structures (50–250 nm in diameter, depending on sequence) fit better with our complementary DLS results—no agglomeration effect of individual 5–20 nm ice artifacts is needed anymore to reconcile the sizes measured by EM and DLS

Growth‐Factor Free Multicomponent Nanocomposite Hydrogels That Stimulate Bone Formation

Synthetic osteo‐promoting materials that are able to stimulate and accelerate bone formation without the addition of exogenous cells or growth factors represent a major opportunity for an aging world population. A co‐assembling system that integrates hyaluronic acid tyramine (HA‐Tyr), bioactive peptide amphiphiles (GHK‐Cu2+), and Laponite (Lap) to engineer hydrogels with physical, mechanical, and biomolecular signals that can be tuned to enhance bone regeneration is reported. The central design element of the multicomponent hydrogels is the integration of self‐assembly and enzyme‐mediated oxidative coupling to optimize structure and mechanical properties in combination with the incorporation of an osteo‐ and angio‐promoting segments to facilitate signaling. Spectroscopic techniques are used to confirm the interplay of orthogonal covalent and supramolecular interactions in multicomponent hydrogel formation. Furthermore, physico‐mechanical characterizations reveal that the multicomponent hydrogels exhibit improved compressive strength, stress relaxation profile, low swelling ratio, and retarded enzymatic degradation compared to the single component hydrogels. Applicability is validated in vitro using human mesenchymal stem cells and human umbilical vein endothelial cells, and in vivo using a rabbit maxillary sinus floor reconstruction model. Animals treated with the HA‐Tyr‐HA‐Tyr‐GHK‐Cu2+ hydrogels exhibit significantly enhanced bone formation relative to controls including the commercially available Bio‐Oss